Filters
▼Clonality
▼Type
▼Reactivity
▼Gene Name
▼Isotype
▼Host
▼Application
▼Clone
▼Active Proteins
AAA Biotech also known as AAA Bio or AAABio provides a variety of high-quality recombinant and natural/native proteins that are proven to work in a wide range of experiments. Explore our products to find the active protein that best fits your needs or experimental model.
Viewing 1-50 of 2567 product results
Bioactivity
(Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-3 (stromelysin-1), can degrade a broad range of substrates including collagen alpha chains, aggrecan, laminin, fibronectin, and elastin. MMP-3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. MMP-3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP-3 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain. The activity of recombinant human MMP-3 is measured by its ability to cleave a fluorogenic peptide substrate Mca-Arg-Pro-Lys-Pro-Val-Glu-Nval-Trp-Arg-Lys(Dnp)-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rhMMP3 is diluted to 200 ug/ml in assay buffer, then activated with 5 ug/ml chymotrypsin at 37 degree C for 30min followed by adding 2 mM PMSF to stop activation. The activated rhMMP3 is diluted to 6.25 ug/mL in assay buffer. Loading into a black well plate 50 uL of 6.25 ug/mL rhMMP3 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhMMP3. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human MMP3 is > 90 pmol/min/ug.)
Matrix Metalloproteinase 3 (MMP3), Active Protein (Cat# AAA161687)
Full Name
Active Matrix Metalloproteinase 3 (MMP3)
Gene Names
MMP3; SL-1; STMY; STR1; CHDS6; MMP-3; STMY1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Stem cell factor (SCF), also known as mast cell growth factor (MGF), and steel factor (SLF), plays an important role in hematopoiesis, spermatogenesis and melanogenesis. SCF has been shown to stimulate the proliferation of TF-1 cells. To test this effect, TF-1 cells were seeded into triplicate wells of 96-well plates at a density of 2 x 104 cells/well and incubated for 72h in the presence or absence of various concentrations of SCF at 37 degree CThe growth of cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8(CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then measure the absorbance at 450 nm using a microplate reader after incubating the plate for 1-4 hours at 37 degree C. Cell proliferation of TF-1 cells after incubation with SCF for 72h observed by inverted microscope was shown in Figure 1. The dose-effect curve of SCF was shown in Figure 2. It was obvious that it significantly promoted cell proliferation of TF-1 cells. The ED50 for this effect is typically 3.9 ng/ml.)
Stem Cell Factor (SCF), Active Protein (Cat# AAA161693)
Full Name
Active Stem Cell Factor (SCF)
Gene Names
KITLG; SF; MGF; SCF; FPH2; KL-1; Kitl; SHEP7
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Collagen Type I Alpha 2 (COL1a2) is a major component of collagen type I found in skin, bone, muscle, tendons, ligaments and other connective tissues.The COL1a2 protein is essential for the assembly, secretion, and stability of collagen fibers, which are vital for tissue development and repair.Mutations in COL1A2 are associated with a variety of genetic disorders, such as osteogenesis imperfecta (dysplasia of the bones) and cutis laxa. These diseases are often accompanied by weak bones and loss of skin elasticity. Besides, Fibrillin 1 (FBN1) has been identified as an interactor of COL1a2, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat COL1a2 and recombinant human FBN1. Briefly, COL1a2 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FBN1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-COL1a2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant rat COL1a2 and recombinant human FBN1 was shown in Figure 1, the EC50 for this effect is 2.53 ug/mL.)
Collagen Type I Alpha 2 (COL1a2), Active Protein (Cat# AAA161716)
Full Name
Active Collagen Type I Alpha 2 (COL1a2)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Application Data
LIF, Active Protein (Cat# AAA214320)
Full Name
Recombinant Mouse LIF
Purity
>95% as determined by SDS-PAGE
Pricing
SDS-PAGE
Interleukin 17C (IL17C), Active Protein (Cat# AAA148226)
Full Name
Active Interleukin 17C (IL17C)
Gene Names
IL17C; CX2; IL-17C
Reactivity
Human
Applications
Activity Assay, Cell Culture
Purity
> 95%
Pricing
Application Data
(Figure.The chemotactic effect of IL8 on Jurkat cells.)
Interleukin 8, Active Protein (Cat# AAA150064)
Full Name
Active Interleukin 8 (IL8)
Gene Names
CXCL8; IL8
Applications
Activity Assay, Cell Culture
Purity
>95%
Pricing
Application Data
IL1A, Active Protein (Cat# AAA214229)
Full Name
Recombinant Human IL1A
Gene Names
IL1A; IL1; IL-1A; IL1F1; IL1-ALPHA
Purity
>95% as determined by SDS-PAGE
Pricing
Bioactivity
(Fibroblast Growth Factor 19 (FGF19) is a member of the fibroblast growth factor (FGF) family. FGF19 has important roles as a hormone produced in the ileum in response to bile acid absorption, regulates new bile acid synthesis, acting through the FGFR4/Klo)
Fibroblast Growth Factor 19 (FGF19), Active Protein (Cat# AAA153122)
Full Name
Active Fibroblast Growth Factor 19 (FGF19)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Fibrinogen Beta Chain (FGB) is the beta subunit of the coagulation factor fibrinogen, which is a component of the blood clot. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. Studies have shown that fibrinogen can enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Thus a functional ELISA assay was conducted to detect the interaction of recombinant mouse FGB and recombinant human ITGb3. Briefly, FGB was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to ITGb3-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FGB pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630nm immediately. The binding activity of recombinant mouse FGB and recombinant human ITGb3 was shown in Figure 1, the EC50 for this effect is 0.016 ug/mL.)
Fibrinogen Beta Chain (FGB), Active Protein (Cat# AAA161834)
Full Name
Active Fibrinogen Beta Chain (FGB)
Gene Names
Fgb; 2510049G14Rik
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Carbonic Anhydrase (CA) catalyzes the reversible reaction of CO2 H2O = HCO3- H, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. Carbonic Anhydrase VB encoded by the CA5B gene is a mitochondrial protein. In comparison with another mitochondrial CA (CA5A), CA5B has different tissue distribution and chromosomal location. The activity of recombinant human CA5B was measured by its ability to hydrolyze 4-Nitrophenyl acetate (4-NPA) to 4-Nitrophenol. The reaction was performed in 12.5 mM Tris, 75 mM NaCl, pH 7.5 (assay buffer), initiated by addition 50 uL of various concentrations of CA5B (diluted by assay buffer) to 50 uL of 2 mM substrate 4-NPA (100 mM stock in Acetone, diluted by assay buffer). Incubated at 37 degree C for 5min, then read at a wavelength of 400 nm.)
Carbonic Anhydrase VB, Mitochondrial (CA5B), Active Protein (Cat# AAA161903)
Full Name
Active Carbonic Anhydrase VB, Mitochondrial (CA5B)
Gene Names
CA5B; CA-VB
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Retinol-binding protein 4 (RBP4) is the specific carrier for retinol (also known as vitamin A), and is responsible for the conversion of unstable and insoluble retinol in aqueous solution into stable and soluble complex in plasma through their tight interaction. As a member of the lipocalin superfamily, RBP4 containing a beta-barrel structure with a well-defined cavity is secreted from the liver, and in turn delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP4-retinol complex interacts with transthyretin (TTR), and this binding is crucial for preventing RBP4 excretion through the kidney glomeruli. RBP4 expressed from an ectopic source efficiently delivers retinol to the eyes, and its deficiency affects night vision largely. Recently, RBP4 as an adipokine, is found to be expressed in adipose tissue and correlated with obesity, insulin resistance (IR) and type 2 diabetes (T2DM). The activity of recombinant bovine RBP4 was measured by its ability to bind all-trans retinoic acid. The binding of retinoic acid results in the quenching of Trp fluorescence in RBP4. RBP4 was diluted to 50 ug/ml in 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, pH 7.5 (assay buffer) and the retinoic acid was diluted to 800, 400, 200, 100, 30, 10, 3, 1, 0.5 and 0.1 uM in 95% ethanol. Mixing 112.5 uL of 50 ug/mL rbRBP4 and 12.5 uL of retinoic acid serial dilutions in microtubes and a blank containing 112.5 uL of 50 ug/mL rbRBP4 and 12.5 uL of 95% ethanol, then incubate at room temperature for 30 minutes. Loading 100 ul of the reaction mixtures and blank and read at excitation and emission wavelengths of 280 nm and 340 nm (top read), respectively, in endpoint mode. The result was shown in figure 1, the 50% binding concentration (BC50) is >190 uM.)
Retinol Binding Protein 4 (RBP4), Active Protein (Cat# AAA161803)
Full Name
Active Retinol Binding Protein 4 (RBP4)
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
WB (Western Blot)
Programmed Cell Death 1 Ligand 1, Active Protein (Cat# AAA174604)
Full Name
Recombinant Mouse Programmed Cell Death 1 Ligand 1 Protein
Gene Names
Cd274; B7h1; Pdl1; Pdcd1l1; Pdcd1lg1; A530045L16Rik
Purity
>95% as determined by reducing SDS-PAGE.
Pricing
SDS-PAGE
Platelet Derived Growth Factor Subunit A (PDGFA), Active Protein (Cat# AAA149234)
Full Name
Active Platelet Derived Growth Factor Subunit A (PDGFA)
Gene Names
PDGFA; PDGF1; PDGF-A
Applications
Activity Assay, Cell Culture
Purity
> 90%
Pricing
WB (Western Blot)
(Western Blot; Sample: Recombinant GSTp, HumanAntibody: Rabbit Anti-Human GSTp Ab )
Glutathione S Transferase Pi (GSTp), Active Protein (Cat# AAA148150)
Full Name
Active Glutathione S Transferase Pi (GSTp)
Applications
Invitro Assay, Activity Assay, Cell Culture
Purity
>95%
Pricing
SDS-PAGE
(Figure 2. SDS-PAGESample: Active recombinant VDR, Human)
Vitamin D Receptor (VDR), Active Protein (Cat# AAA148172)
Full Name
Active Vitamin D Receptor (VDR)
Gene Names
VDR; NR1I1; PPP1R163
Reactivity
Homo sapiens (Human)
Applications
Activity Assay, Cell Culture
Purity
>92%
Pricing
SDS-PAGE
Hypoxia Inducible Factor 1 Alpha (HIF1a), Active Protein (Cat# AAA148241)
Full Name
Active Hypoxia Inducible Factor 1 Alpha (HIF1a)
Gene Names
HIF1A; HIF1; MOP1; PASD8; HIF-1A; bHLHe78; HIF-1alpha; HIF1-ALPHA; HIF-1-alpha
Reactivity
Human
Applications
Activity Assay, Cell Culture
Purity
> 95%
Pricing
SDS-PAGE
Interleukin-36 alpha protein (Il36a), Active Protein (Cat# AAA114251)
Full Name
Recombinant Mouse Interleukin-36 alpha protein (Il36a) (Active)
Gene Names
Il1f6; Fil1; Il1f9; Il36a; IL-1H1; IL1RP2
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Carbonic Anhydrase 1 (CA1), Active Protein (Cat# AAA235617)
Full Name
Recombinant Human Carbonic Anhydrase 1 (CA1)
Gene Names
CA1; CAB; CA-I; Car1; HEL-S-11
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Application Data
Glutathione S Transferase Mu 1 (GSTm1), Active Protein (Cat# AAA148176)
Full Name
Active Glutathione S Transferase Mu 1 (GSTm1)
Gene Names
Gstm1; GSTA3
Reactivity
Rat
Applications
Activity Assay, Cell Culture
Purity
> 95%
Pricing
SDS-PAGE
Stromal Cell Derived Factor 1 (SDF1), Active Protein (Cat# AAA148247)
Full Name
Active Stromal Cell Derived Factor 1 (SDF1)
Gene Names
CXCL12; IRH; PBSF; SDF1; TLSF; TPAR1; SCYB12
Reactivity
Human
Applications
Activity Assay, Cell Culture
Purity
> 95%
Pricing
Bioactivity
(Homing Associated Cell Adhesion Molecule (HCAM), also known as CD44, is a ubiquitous multistructural and multifunctional cells surface adhesion molecule involved in cell-cell and cell-matrix interactions. CD44 is broadly expressed, including in the membranes of B cells, granulocytes, monocytes, and erythrocytes as well as on many thymocytes and mature T cells, besides it is highly expressed in many cancers and regulates metastasis via recruitment of CD44 to the cell surface. This protein is a receptor for hyaluronic acid (HA) and can also interact with other ligands, such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse HCAM and biotinylated hyaluronan (HA). Briefly, biotin-linked HA was diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to HCAM-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 1 hour, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant mouse HCAM and biotinylated HA was shown in Figure 1, and this effect was in a dose dependent manner.)
Homing Associated Cell Adhesion Molecule (HCAM), Active Protein (Cat# AAA161765)
Full Name
Active Homing Associated Cell Adhesion Molecule (HCAM)
Gene Names
Cd44; Ly-24; Pgp-1; HERMES; AU023126; AW121933; AW146109
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(CLEC3B (Ctype lectin domain family 3 member B), also known as Tetranectin (TN), is a plasminogen-kringle-4-binding protein that is detected in various endocrine tissues and in epithelial and mesenchymal cells, including fibroblasts, monocytes, and neutrophils. Studies have shown that abnormal CLEC3B expression plays an important role in tumourigenesis and metastasis in gastric adenocarcinoma, breast cancer, cervical cancer, ovarian cancer, carcinoma of the urinary bladder, and melanoma. Besides, Secreted Phosphoprotein 2 (SPP2) has been identified as an interactor of CLEC3B, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human SPP2 and recombinant human CLEC3B. Briefly, CLEC3B was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to SPP2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CLEC3B pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human CLEC3B and recombinant human SPP2 was shown in Figure 1, the EC50 for this effect is 0.08 ug/mL.)
C-Type Lectin Domain Family 3, Member B (CLEC3B), Active Protein (Cat# AAA161934)
Full Name
Active C-Type Lectin Domain Family 3, Member B (CLEC3B)
Gene Names
CLEC3B; TN; TNA
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Beta-Nerve Growth Factor (NGF), Active Protein (Cat# AAA235613)
Full Name
Recombinant Human Beta-nerve growth factor (NGF) (Active)
Gene Names
NGF; NGFB; HSAN5; Beta-NGF
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Interleukin-7 (IL7), Active Protein (Cat# AAA235615)
Full Name
Recombinant Human Interleukin-7 (IL7)
Gene Names
IL7; IL-7
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Interleukin-15 & Interleukin-15 Receptor Subunit alpha (IL15 & IL15RA), Active Protein (Cat# AAA235616)
Full Name
Recombinant Human Interleukin-15 & Interleukin-15 Receptor Subunit alpha (IL15 & IL15RA)
Gene Names
IL15RA; CD215
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Pricing
Bioactivity
(Fibroblast Growth Factor 12 (FGF12) is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. Fibroblast Growth Factor 12 (FGF12) may represent an important modulator of neuronal network activity and has been associated with developmental and epileptic encephalopathy (DEE). Besides, it is reported that both domains of (Ca2)4-CaM directly bind two sites in the N-terminal domain (NTD) of A-type FGF splice variants (FGF11A, FGF12A, FGF13A, and FGF14A) with high affinity. Calmodulin 1 (CALM1) has been identified as an interactor of FGF12, thus a binding ELISA assay was conducted to detect the interaction of recombinant human FGF12 and recombinant human CALM1. Briefly, FGF12 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to CALM1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FGF12 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630nm immediately. The binding activity of recombinant human FGF12 and recombinant human CALM1 was shown in Figure 1, the EC50 for this effect is 4.44 ug/mL.)
Fibroblast Growth Factor 12 (FGF12), Active Protein (Cat# AAA161897)
Full Name
Active Fibroblast Growth Factor 12 (FGF12)
Gene Names
FGF12; FHF1; FGF12B
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Carbonic Anhydrase (CA) catalyzes the reversible reaction of CO2 H2O = HCO3- H, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. CA3 is a cytosolic enzyme with a very low CA activity. It is expressed at low levels in human muscle during early development but increases rapidly during the last trimester to reach 50-60% of adult levels at birth. The activity of recombinant human CA3 was measured by its ability to hydrolyze 4-Nitrophenyl acetate (4-NPA) to 4-Nitrophenol. The reaction was performed in 12.5 mM Tris, 75 mM NaCl, pH 7.5 (assay buffer), initiated by addition 50 uL of various concentrations of CA3 (diluted by assay buffer) to 50 uL of 2 mM substrate 4-NPA (100 mM stock in Acetone, diluted by assay buffer). Incubated at 37 degree C for 5min, then read at a wavelength of 400 nm.)
Carbonic Anhydrase III, Muscle Specific (CA3), Active Protein (Cat# AAA161899)
Full Name
Active Carbonic Anhydrase III, Muscle Specific (CA3)
Gene Names
CA3; Car3; CAIII
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Glypican 5 (GPC5) belongs to the glypican family of proteoglycans that are linked to the cell surface through a glycosyl-phosphatidylinositol anchor. GPC5 is expressed primarily in embryonic neurons and mesenchyme and it is implicated in a variety of physiological processes, ranging from cell proliferation to morphogenesis. Besides, Syndecan 1 (SDC1) has been identified as an interactor of GPC5, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat GPC5 and recombinant human SDC1. Briefly, GPC5 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to SDC1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GPC5 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant rat GPC5 and recombinant human SDC1 was shown in Figure 1, the EC50 for this effect is 0.6 ug/mL.)
Glypican 5 (GPC5), Active Protein (Cat# AAA161913)
Full Name
Active Glypican 5 (GPC5)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Ephrin-A1 (EFNA1), also known as EPLG1, LERK1, TNFAIP4, Immediate early response protein B61, is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. EFNA1 plays an important role in angiogenesis and tumor neovascularization. EFNA1 widely affects tumor growth through enhancing tumor angiogenesis, malignant cell events and invasiveness. Ephrin Type A Receptor 1 (EPHA1) is one of high-affinity ligands for EFNA1, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human EFNA1 and recombinant mouse EPHA1. Briefly, biotin-linked EFNA1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to EPHA1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of recombinant human EFNA1 and recombinant mouse EPHA1 was shown in Figure 1, the EC50 for this effect is 0.24 ug/mL.)
Ephrin A1 (EFNA1), Active Protein (Cat# AAA161914)
Full Name
Active Ephrin A1 (EFNA1)
Gene Names
EFNA1; B61; EFL1; ECKLG; EPLG1; LERK1; LERK-1; TNFAIP4
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Ephrin A2 (EFNA2) is a cell surface-associated protein belonging to the Ephrin family, which are involved in intercellular communication and cell localization. EFNA2 is mainly expressed in tissues including the brain, heart, lung, kidney and pancreas. And this protein is involved in regulating a variety of biological processes, including cell migration, cell differentiation, and tissue boundary formation, by interacting with Eph receptors. It aslo plays a significant role in the development and maintenance of the cardiovascular system, as well as in the regulation of synaptic plasticity and neuronal circuitry in the brain. A Disintegrin And Metalloprotease 10 (ADAM10), a disintegrin and metalloproteinase, can cleave EFNA2, potentially altering the activity of EFNA2 or its interaction with Eph receptors, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human EFNA2 and recombinant rat ADAM10. Briefly, biotin-linked EFNA2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to ADAM10-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of EFNA2 and ADAM10 was shown in Figure 1, the EC50 for this effect is 1.38 ug/mL.)
Ephrin A2 (EFNA2), Active Protein (Cat# AAA161915)
Full Name
Active Ephrin A2 (EFNA2)
Gene Names
EFNA2; ELF-1; EPLG6; LERK6; HEK7-L; LERK-6
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Ephrin-A4, also known as EFNA4 and EFL-4, is a member of the ligand of the EPH family. It is mainly expressed in the spleen, lymph nodes, ovary, small intestine and colon of adults, as well as in the heart, lungs, liver, and kidneys of the fetus. It is involved in the development of neurons, blood vessels, and epithelium by regulating cell migration, rejection, and adhesion. Ephrin-A4 has been shown to bind FYN,EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant rat EFNA4 and recombinant human FYN. Briefly, EFNA4 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FYN-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-EFNA4 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant rat EFNA4 and recombinant human FYN was shown in Figure 1, the EC50 for this effect is 0.37 ug/mL.)
Ephrin A4 (EFNA4), Active Protein (Cat# AAA161918)
Full Name
Active Ephrin A4 (EFNA4)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(To test the effect of MIA1 on cell apoptosis, A375 cells were seeded into triplicate wells of 96-well plates at a density of 4,000 cells/well and allowed to attach overnight, then the medium was replaced with various concentrations of recombinant human MIA1 diluted with 5% serum standard DMEM. After incubated for 48h, cells were observed by inverted microscope and cell viability was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10 ul of CCK-8 solution was added to each well of the plate, then the absorbance at 450 nm was measured using a microplate reader after incubating the plate for 1-4 hours at 37 degree C. Apoptosis of A375 cells after incubation with MIA1 for 48h observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 assay after incubation with recombinant human MIA1 for 48h. The result was shown in Figure 2. It was obvious that MIA1 significantly decreased cell viability of A375 cells. The ED50 of recombinant human MIA1 is 0.53 ug/ml.)
Melanoma Inhibitory Activity Protein 1 (MIA1), Active Protein (Cat# AAA161926)
Full Name
Active Melanoma Inhibitory Activity Protein 1 (MIA1)
Gene Names
MIA; CD-RAP
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Cystatin D is a member of family 2 of the cystatin superfamily. In contrast to other members of family 2, Cystatin D has restricted tissue distribution and has been found only in saliva and tears. Two allelic variants (Arg46 and Cys46) are known in the human protein and they are not significantly different in their inhibitory activity against papain and cathepsins B, H, L and S. Recombinant Human Cystatin D corresponds to the Arg46 variant. The functions of Cystatin D are largely unknown. However, Cystatin D has been shown to inhibit coronavirus replication at its physiological concentration (0.121.9 uM) and has been suggested to play a protective role against proteases present in the oral cavity. The activity of recombinant human Cystatin D was measured by its ability to inhibit papain cleavage of a fluorogenic peptide substrate Z-FR-AMC in the assay buffer 50 mM Tris, pH 7.0. Papain was diluted to 500 ug/ml in activation buffer 50 mM Tris, 5 mM DTT, pH 7.0 and incubated at room temperature for 15 minutes. The activated papain was diluted to 100 ug/ml in the assay buffer and 20 ul different concentrations of recombinant human Cystatin D (MW: 17.45 KD) was incubated with 20 ul 100 ug/ml papain at 37 degree C for 10 minutes. Loading 50 uL of the incubated mixtures which were diluted five-fold in assay buffer into empty wells of a plate, and start the reaction by adding 50 uL of 200 uM substrate. Include a substrate blank containing 50 uL of assay buffer and 50 uL of 200 uM substrate. Then read at excitiation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant human Cystatin D significantly decreased papain activity. The inhibition IC50 was )
Cystatin 5 (CST5), Active Protein (Cat# AAA161930)
Full Name
Active Cystatin 5 (CST5)
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Sequence
Steroid 5 Alpha Reductase 1 (SRD5a1), Active Protein (Cat# AAA161940)
Full Name
Active Steroid 5 Alpha Reductase 1 (SRD5a1)
Gene Names
Srd5a1; S5AR 1; Srd5a-1; 0610031P22Rik; 4930435F02Rik
Applications
Activity Assay
Purity
>80%
Pricing
Bioactivity
(Human TFPI, also known as lipoprotein-associated coagulation inhibitor (LACI) and extrinsic pathway inhibitor (EPI), is a physiological inhibitor of extrinsic pathway of coagulation and has biological functions of anticoagulation and anti-inflammation. It is a secreted protein with a N-terminal acidic region, three Kunitz (K) domains separated with by two linker regions, and a C-terminal basic region. The activity of recombinant human TFPI was measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate Mca-RPKPVE-Nval-WRK(Dnp)-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. Trypsin was diluted to 50 ug/ml in the assay buffer and 20 ul different concentrations of recombinant human TFPI (MW: 55.58 KD) was incubated with 20 ul diluted trypsin at 37 degree C for 15 minutes. Loading 50 uL of the incubated mixtures which were diluted five-fold in assay buffer into empty wells of a plate, and start the reaction by adding 50 uL of 20 uM substrate. Include a substrate blank containing 50 uL of assay buffer and 50 uL of 20 uM substrate. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant human TFPI significantly decreased trypsin activity. The inhibition IC50 was )
Tissue Factor Pathway Inhibitor (TFPI), Active Protein (Cat# AAA161731)
Full Name
Active Tissue Factor Pathway Inhibitor (TFPI)
Gene Names
TFPI; EPI; TFI; LACI; TFPI1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
SDS-PAGE
(Sample: Active recombinant EMILIN1, Human)
Elastin Microfibril Interface Located Protein 1 (EMILIN1), Active Protein (Cat# AAA161733)
Full Name
Active Elastin Microfibril Interface Located Protein 1 (EMILIN1)
Gene Names
EMILIN1; EMI; gp115; EMILIN
Reactivity
Homo sapiens (Human)
Applications
Activity Assay
Purity
>80%
Pricing
Bioactivity
(Luteinizing Hormone (LH) is a 42 kDa heterodimer belonging to the glycoprotein hormone family. It is composed of noncovalently linked glycosylated alpha and beta chains. The alpha subunit (CG alpha) is also a component of Follicle-Stimulating Hormone (FSH), Thyroid-Stimulating Hormone, and Chorionic Gonadotropin. The unique beta subunit confers the protein's specific biological action and is responsible for the interaction with its receptor. LH is produced and secreted by the anterior pituitary gland. Its secretion is controlled by Gonadotropin-Releasing Hormone from the hypothalamus; however, LH secretion can also be stimulated by estradiol. A functional binding ELISA assay was conducted to detect the interaction of recombinant human CGa/LHb and recombinant human Dopamine Receptor D1 (DRD1). Briefly, biotin-linked CGa/LHb were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to DRD1-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of CGa/LHb and DRD1 was shown in Figure 1, the EC50 for this effect is 0.644 ug/mL.)
Luteinizing Hormone (LH), Active Protein (Cat# AAA161734)
Full Name
Active Luteinizing Hormone (LH)
Gene Names
CGA; HCG; LHA; FSHA; GPHa; TSHA; GPHA1; CG-ALPHA
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Serpin B2, also known as PAI-2, is an approximately 60 kDa serine protease inhibitor. It is primarily secreted by macrophages and monocytes and can form disulfide-linked multimers. Serpin B2 inhibits both the urokinase-type and tissue-type plasminogen activators (uPA and tPA). Serpin B2 also promotes the clearance of uPA by enhancing its binding and uptake by LRP. It limits fibril formation by Huntington protein (HTT) and beta-Amyloid peptides. It promotes Th2 biased immune responses and is important for intestinal CCL2 production, monocyte recruitment, and nematode clearance. A non-glycosylated form of Serpin B2 is retained intracellularly where it interferes with TNF-a induced apoptosis by protecting the Retinoblastoma protein (RB1) from calpain digestion. It also inhibits proteasome activity in activated endothelial cells. The activity of recombinant mouse PAI-2 was measured by its ability to inhibit uPA cleavage of a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC) in the assay buffer 50 mM Tris, 0.01% Tween 20, pH 8.5. The 50 ul different concentrations of rmPAI-2 (MW: 47.9 KD) was incubated with 50ul 2ug/ml rhuPA (EPA140Mu61) at room temperature for 15 minutes. Loading 50 uL of the incubated mixtures into empty wells of a plate, and start the reaction by adding 50 uL of 200 uM substrate (Z-GGR-AMC). Include a substrate blank containing 50 uL of assay buffer and 50 uL of 200 uM substrate. Then read at excitiation and emission wavelengths of 380 nm and 460 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that PAI2 significantly decreased uPA activity. The inhibition IC50 was )
Plasminogen Activator Inhibitor 2 (PAI2), Active Protein (Cat# AAA161740)
Full Name
Active Plasminogen Activator Inhibitor 2 (PAI2)
Gene Names
Serpinb2; PAI-2; Planh2; ovalbumin
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Tissue inhibitors of metalloproteinase 1 (TIMP1) is a member of the family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). TIMP-1 is a glycoprotein with a molecular mass of 28 kDa produced by a wide range of cell types. TIMP-1 inhibits active MMP-mediated proteolysis by forming an N-terminal, non-covalent binary complex with the MMP active site. The activity of recombinant dog TIMP1 was measured by its ability to inhibit rhMMP2 cleavage of a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. rhMMP2 was diluted to 100 ug/ml and activated with 1 mM APMA at 37 degree C for 1 hour and TIMP1 (MW: 20.86 KD) was diluted to different concentrations with the assay buffer. Mix 8 ul of TIMP1 curve dilutions, 12.8 ul of activated rhMMP-2, and 59.2 ul of assay buffer, including a control containing assay buffer and the diluted rhMMP-2 and incubate the reactions for 2 hours at 37 degree C. Loading 50 ul of the incubated mixtures which were diluted five-fold in assay buffer into empty wells of a plate, and start the reaction by adding 50 ul of 20 uM substrate. Include a substrate blank containing 50 ul of assay buffer and 50 ul of 20 uM substrate. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The result was shown in Figure 1 and it was obvious that recombinant dog TIMP1 significantly decreased rhMMP2 activity. The inhibition IC50 was )
Tissue Inhibitors Of Metalloproteinase 1 (TIMP1), Active Protein (Cat# AAA161742)
Full Name
Active Tissue Inhibitors Of Metalloproteinase 1 (TIMP1)
Gene Names
TIMP1; TIMP-1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. The activity of recombinant human MMP9 is measured by its ability to cleave a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rhMMP9 is diluted to 100 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 degree C for 1 hours. The activated rhMMP9 is diluted to 0.2 ug/mL in assay buffer. Loading into a black well plate 50 uL of 0.2 ug/mL rhMMP9 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhMMP9. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human MMP9 is > 3000 pmol/min/ug.)
Matrix Metalloproteinase 9 (MMP9), Active Protein (Cat# AAA161746)
Full Name
Active Matrix Metalloproteinase 9 (MMP9)
Gene Names
MMP9; GELB; CLG4B; MMP-9; MANDP2
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Homing Associated Cell Adhesion Molecule (HCAM), also known as CD44, is a ubiquitous multistructural and multifunctional cells surface adhesion molecule involved in cell-cell and cell-matrix interactions. CD44 is broadly expressed, including in the membranes of B cells, granulocytes, monocytes, and erythrocytes as well as on many thymocytes and mature T cells, besides it is highly expressed in many cancers and regulates metastasis via recruitment of CD44 to the cell surface. This protein is a receptor for hyaluronic acid (HA) and can also interact with other ligands, such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant mouse HCAM and biotinylated hyaluronan (HA). Briefly, biotin-linked HA was diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to HCAM-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 1 hour, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant mouse HCAM and biotinylated HA was shown in Figure 1, and this effect was in a dose dependent manner.)
Homing Associated Cell Adhesion Molecule (HCAM), Active Protein (Cat# AAA161764)
Full Name
Active Homing Associated Cell Adhesion Molecule (HCAM)
Gene Names
Cd44; Ly-24; Pgp-1; HERMES; AU023126; AW121933; AW146109
Applications
Activity Assay, Cell Culture
Purity
Greater than 80% by SDS-PAGE
Pricing
Bioactivity
(Tissue kallikreins are a family of extracellular serine proteases consisting of 15 members. Tissue kallikreins have attracted great interest as potential biomarkers for various cancers, including prostate, ovarian, breast, testicular, and lung. Human Kallikrein 6 (hKLK6) is a member of tissue kallikrein family observed in breast and brain tissues, colon carcinoma cells, and oligodedrocytes. Known protein substrates of hKLK6 are myelin basic protein, the precursor of the A beta amyloid peptide, and plasminogen. Its physiological functions may include the participation in demyelination processes as well as in the progression of inflammatory disease of the CNS. The activity assay of recombinant mouse KLK6 was measured by its ability to cleave the fluorogenic peptide substrate Boc-QAR-AMC. The rmKLK6 was activated by Lysyl-endopeptidase in the activation buffer 50 mM Tris, 0.05% (w/v) Brij-35, pH 8.0, of which equal volumes of 200 ug/ml rmKLK6 and 2.5 mU/ml Lysyl-endopeptidase were combined and incubated at room temperature for 30 minutes. The activated rmKLK6 was diluted to 3 ug/ml in assay buffer and start the reaction by adding 50 uL of 200 uM substrate. Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes. The specific activity of recombinant mouse KLK6 is >6000 pmol/min/ug.)
Kallikrein 6 (KLK6), Active Protein (Cat# AAA161769)
Full Name
Active Kallikrein 6 (KLK6)
Gene Names
Klk6; BSP; MSP; Bssp; Klk29; Prss9; Prss18; AI849898; neurosin
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(C reactive protein (CRP) is an annular (ring-shaped), pentameric protein found in blood plasma, whose levels rise in response to inflammation. It is an acute-phase protein of hepatic origin that increases following interleukin-6 secretion by macrophages and T cells. Its physiological role is to bind to lysophosphatidylcholine expressed on the surface of dead or dying cells (and some types of bacteria) in order to activate the complement system via C1q. Besides, Coagulation Factor II (F2) has been identified as an interactor of CRP, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant dog CRP and recombinant rat F2. Briefly, CRP was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to F2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CRP pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant dog CRP and recombinant rat F2 was shown in Figure 1, the EC50 for this effect is 0.82 ug/mL.)
C ReProtein (CRP), Active Protein (Cat# AAA161778)
Full Name
Active C Reactive Protein (CRP)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(PRL (prolactin), also known as luteotropin, is a hormone secreted from the pituitary gland and is best known for its role in enabling mammals to produce milk. PRL plays an essential role in metabolism, regulation of the immune system through activating its specific membrane-anchored receptor (PRLR). A functional ELISA assay was conducted to detect the interaction of recombinant bovine PRL and recombinant human PRLR. Briefly, PRL was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PRLR-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PRL pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant bovine PRL and recombinant human PRLR was shown in Figure 1, the EC50 for this effect is 0.05 ug/mL.)
Prolactin (PRL), Active Protein (Cat# AAA161787)
Full Name
Active Prolactin (PRL)
Gene Names
PRL; GHA1; Prol
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(PRL (prolactin), also known as luteotropin, is a hormone secreted from the pituitary gland and is best known for its role in enabling mammals to produce milk. PRL plays an essential role in metabolism, regulation of the immune system through activating its specific membrane-anchored receptor (PRLR). A functional binding ELISA assay was conducted to detect the interaction of recombinant horse PRL and recombinant human PRLR. Briefly, PRL was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PRLR-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PRL pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant horse PRL and recombinant human PRLR was shown in Figure 1, the EC50 for this effect is 0.11 ug/mL.)
Prolactin (PRL), Active Protein (Cat# AAA161789)
Full Name
Active Prolactin (PRL)
Gene Names
PRL; GHA1
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Pricing
Bioactivity
(Carbonic Anhydrase (CA) catalyzes the reversible reaction of CO2 H2O = HCO3- H, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. CA1 is a cytosolic enzyme with the highest levels in erythrocytes and is a very early marker for erythroid differentiation. The activity of recombinant human CA1 was measured by its ability to hydrolyze 4-Nitrophenyl acetate (4-NPA) to 4-Nitrophenol. The reaction was performed in 12.5 mM Tris, 75 mM NaCl, pH 7.5 (assay buffer), initiated by addition 50 uL of various concentrations of CA1 (diluted by assay buffer) to 50 uL of 2 mM substrate 4-NPA (100 mM stock in Acetone, diluted by assay buffer). Incubated at 37 degree C for 5min, then read at a wavelength of 400 nm.)
Carbonic Anhydrase I (CA1), Active Protein (Cat# AAA161796)
Full Name
Active Carbonic Anhydrase I (CA1)
Gene Names
CA1; CAB; CA-I; Car1
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Peroxisome Proliferator Activated Receptor Gamma (PPARg) belongs to a large group of nuclear receptors controlling reproduction, metabolism, development and immune response. It is mainly expressed in adipose tissue, hematopoietic cells and the large intestine and it plays an important role in adipocyte differentiation, lipid and glucose metabolism, and modulation of immune and inflammatory reactions. Besides, Peroxisome Proliferator Activated Receptor Gamma Coactivator 1 Alpha (PPARgC1a) has been identified as an interactor of PPARg, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human PPARg and recombinant mouse PPARgC1a. Briefly, PPARg was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to PPARgC1a-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PPARg pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human PPARg and recombinant mouse PPARgC1a was shown in Figure 1, the EC50 for this effect is 0.03 ug/mL.)
Peroxisome Proliferator Activated Receptor Gamma (PPARg), Active Protein (Cat# AAA161802)
Full Name
Active Peroxisome Proliferator Activated Receptor Gamma (PPARg)
Gene Names
PPARG; GLM1; CIMT1; NR1C3; PPARG1; PPARG2; PPARgamma
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Figure 2. Inhibition of HepG2 cells proliferation after stimulated with recombinant rat BMP4)
Bone Morphogenetic Protein 4 (BMP4), Active Protein (Cat# AAA161655)
Full Name
Active Bone Morphogenetic Protein 4 (BMP4)
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Fibroblast Growth Factor 9 (FGF9) is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. FGF9 secreted by HSC is a candidate activating ligand for hepatocyte FGFR4 functions, thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human FGF9 and recombinant human FGFR4. Briefly, biotin-linked FGF9 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to FGFR4-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30 min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450 nm immediately. The binding activity of FGF9 and FGFR4 was shown in Figure 1, the EC50 for this effect is 0.23 ug/mL.)
Fibroblast Growth Factor 9 (FGF9), Active Protein (Cat# AAA161661)
Full Name
Active Fibroblast Growth Factor 9 (FGF9)
Gene Names
FGF9; GAF; FGF-9; SYNS3; HBFG-9; HBGF-9
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
Bioactivity
(Growth Hormone (GH), also known as somatotropin, is a member of a family of growth factors. Human growth hormone is a 191 amino acid single-chain polypeptide produced via the anterior pituitary of the brain in the acidophilic, somatotrophic cells. Its production is tightly regulated through several complex feedback mechanisms in response to stress, exercise, nutrition, sleep, and growth hormone itself. Annexin A2 (ANXA2) has been shown to play multiple roles in growth, development, metabolism and ANXA2 is a high affinity receptor for GH. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human GH and recombinant human ANXA2. Briefly, GH was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to ANXA2-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GH pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody for 1h at 37 degree C, wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50 ul stop solution to the wells and read at 450/630 nm immediately. The binding activity of recombinant human GH and recombinant human ANXA2 was shown in Figure 1, the EC50 for this effect is 2.1 ug/mL.)
Growth Hormone (GH), Active Protein (Cat# AAA161667)
Full Name
Active Growth Hormone (GH)
Gene Names
GH1; GH; GHN; GH-N; hGH-N; IGHD1B
Applications
Activity Assay, Cell Culture
Purity
Greater than 90% by SDS-PAGE
Pricing
What Are Active Proteins?
Proteins are large molecules made up of long chains of amino acids.
They will typically fold into a very particular 3-dimensional shape/conformation, that is sometimes referred to as their “native” form, which allows them to work properly in the body. For the purposes of product categorization, AAA Biotech will typically refer to proteins purified from their original animal host as being “native” proteins (this is to signify their difference compared to their “recombinant” or “synthetic” protein counterparts).
If a protein successfully folds into the correct shape, it is will typically display high fidelity characteristics to its original protein in its original animal host, and be classified as an active protein, as it will be able to function “normally” in most enzymatic or binding capacities. If it loses this shape, due to factors such as heat or strong chemicals (such as detergents), it becomes inactive and is no longer able to perform its basic functions. All of the proteins in this category are made under strict quality control, and they are active, pure, low in contaminants, and stable.
Most are stored as freeze-dried powders and come without extra tags, so they’re very close to the actual natural/native form.
Key Applications of Active Proteins
1. Scientific Research
- Aid in the study of how proteins function in the body
- Aid in understanding various disease processes
2. Drug Development
- Powerful tools to investigate how potential drugs interact with specific proteins
- Ideal for identifying drug targets
3. Cell Culture
- Are routinely utilized to support cell growth and function (e.g., using exogenous growth factors)
- Can be used to promote cellular development into specific types (differentiation)
4. Diagnostics
- Regularly utilized in tests to detect diseases or infections (e.g., COVID-19, cancer)
- Note: All products are strictly for research-use only (RUO).
5. Therapeutics
- Some active proteins are used directly as treatments (e.g., insulin, enzymes)
- Note: All products are strictly for research-use only (RUO).
6. Vaccine Development
- Used to create or test vaccines by mimicking parts of viruses or bacteria
7. Biochemical Assays
- They can facilitate the characterization of enzyme activity, binding strength, or protein interactions in lab tests
Why Buy Active Proteins from AAA Biotech?
- High biological activity – Verified to perform as expected or indicated on datasheet
- Strict quality control – We are confident in our active proteins’ reliability and consistency
- High purity & low endotoxin – Ideal for applications involving sensitive or precious samples/components
- Freeze-dried for stability – Long shelf life and straightforward storage
- Mostly tag-free – Closer to natural/native protein form
FAQ
1. What are active proteins used for in research?
Active proteins are used primarily in the study of how proteins function, in characterizing/discovering drug interactions, supporting cell growth, running biochemical assays, and in development of diagnostics or therapeutics.
2. How are AAA Biotech's active proteins validated?
AAA Biotech’s active proteins are validated through strict quality control and functional assays to ensure they are properly folded and active. “Active”, though, can be an ambiguous term, so if a specific “activity” or “binding” capability of a protein is of crucial interest to you, please inquire with us prior to purchase, and we will provide further details on how the “Active” modifier was determined to be applicable.
3. Are these proteins tested for biological activity?
Yes, all active proteins from AAA Biotech are tested to confirm they have the expected biological activity before being offered for use. Though, said “biological activity” can be either “enzymatic”, “binding”, or both.