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SDS-PAGE (Figure 2. SDS-PAGESample: Active recombinant CLCA1, Human)
Bioactivity (CLCA1 (Calcium-activated chloride channel regulator 1) is a member of the calcium sensitive chloride conductance protein family. This protein is expressed as a precursor protein that is processed into two cell-surface-associated subunits. It has been reported that CLCA1 activates calcium-dependent chloride channel through the interaction with TMEM16A (anoctamin-1). Besides, there exits similarities between human and mouse TMEM16A in amino acid sequence with the identity of 89.66%. Thus, a functional ELISA assay was conducted to detect the association of recombinant human CLCA1 with recombinant mouse TMEM16A. Briefly, CLCA1 were diluted serially in PBS with 0.01%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to TMEM16A-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CLCA1 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of CLCA1 with TMEM16A was shown in Figure 1 and this effect was in a dose dependent manner.)
Activity (JAK2 (Tyrosine-protein kinase JAK2) is a tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. JAK2 is considered to associate with some type I receptors, including EPOR (Erythropoietin receptor), therefore participates in cellular signal transduction. Thus a binding ELISA assay was conducted to detect the interaction of recombinant human JAK2 and recombinant human EPOR. Briefly, JAK2 were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL JAK2 were then transferred to EPOR-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-JAK2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of JAK2 and EPOR was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (NEU (Sialidase-1) is an enzyme that catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (CTSA). Thus a binding ELISA assay was conducted to detect the interaction of recombinant human NEU and recombinant human CTSA. Briefly, NEU were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to CTSA-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-NEU pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of NEU and CTSA was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Fibronectin (FN) is a high-molecular weight (~440kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectin has numerous functions. For example, it involved in cell adhesion, cell motility, opsonization, wound healing, maintenance of cell shape, and so on. Besides, Connective Tissue Growth Factor (CTGF) has been identified as an interactor of FN, thus a binding ELISA assay was conducted to detect the interaction of recombinant human FN and recombinant human CTGF. Briefly, FN were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to CTGF-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FN pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of FN and CTGF was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Interferon gamma (IFNgamma) is a dimerized soluble cytokine that is the only member of the type II class of interferons. The importance of IFNgamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. It has been reported that IFN-gamma promotes production of inducible Nitric Oxide Synthase (iNOS) in macrophages as an important activator. After stimulated with IFN-gamma, morphological changes will occur in murine macrophage cell line (Raw 264.7 cells), and inducible nitric-oxide synthase (iNOS) in the cells will increase. Raw 264.7 cells were incubated in DMEM with IFN-gamma (10ng/mL) for 24h, then cells were observed by inverted microscope and iNOS in cell lysates was detected by ELISA.Effect of IFN-gamma on morphological change of Raw 246.7 cells was shown in Figure 1.)
Activity (Figure. Cell proliferation of TF-1 cells after stimulated with LIF.Leukemia Inhibitory Factor (LIF), is an interleukin 6 class cytokine that affects cell growth by inhibiting differentiation. Other properties attributed to the cytokine include: the growth promotion and cell differentiation of different types of target cells, influence on bone metabolism, cachexia, neural development, embryogenesis and inflammation. p53 regulated LIF has been shown to facilitate implantation in the mouse model and possibly in humans. To test the effect of LIF on cell proliferation, TF-1 cells were seeded into triplicate wells of 96-well plates at a density of 5,000 cells/well with 1% serum standard 1640 including various concentrations of recombinant human LIF. After incubated for 72h, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10uL of CCK-8 solution was added to each well of the plate, then the absorbance at 450nm was measured using a microplate reader after incubating the plate for 1-4 hours at 37 degree C. Proliferation of TF-1 cells after incubation with LIF for 72h observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 (Cell Counting Kit-8 ) assay after incubation with recombinant LIF for 72h. The result was shown in Figure 2. It was obvious that LIF significantly increased cell viability of TF-1 cells.(A) TF-1 cells cultured in 1640, stimulated with 0.5ng/mL LIF for 72h; (B) Unstimulated TF-1 cells cultured in 1640 for 72h.)
Bioactivity (Paraoxonase 2 which is a member of the paraoxonase family also known as arylesterase 2. PON2 is exclusively intracellularly found, wherein it functions as an anti-oxidative protein by reducing intracellular and local oxidative stress. This protein is ubiquitously expressed in human tissues, membrane-bound, and may act as a cellular antioxidant, protecting cells from oxidative stress. Besides, ATPase, H+ Transporting, Lysosomal Accessory Protein 2 (ATP6AP2) has been identified as an interactor of PON2, thus a binding ELISA assay was conducted to detect the interaction of recombinant human PON2 and recombinant human ATP6AP2. Briefly, PON2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to ATP6AP2-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-PON2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of PON2 and ATP6AP2 was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Figure. The binding activity of SPC with EIF2aK3. Surfactant associated proteins (SPC), is one of the pulmonary surfactant proteins. It is a membrane protein which manufactures surfactant. The propeptide of pulmonary surfactant C has an N-terminal alpha-helical segment whose suggested function was stabilization of the protein structure, since the latter can irreversibly transform from its native alpha-helical structure to beta-sheet aggregates and form amyloid fibrils. Besides, Eukaryotic Translation Initiation Factor 2 Alpha Kinase 3 (EIF2aK3) has been identified as an interactor of SPC, thus a binding ELISA assay was conducted to detect the interaction of recombinant mouse SPC and recombinant mouse EIF2aK3. Briefly, SPC were diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to EIF2aK3-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-SPC pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of SPC and EIF2aK3 was shown in Figure 1, and this effect was in a dose dependent manner.Figure 1. The binding activity of SPC with EIF2aK3.)
Activity (Creatine Kinase, Brain (CKB) consists of a homodimer of two identical brain-type CK-B subunits. CKB is a cytoplasmic enzyme involved in cellular energy homeostasis, with certain fractions of the enzyme being bound to cell membranes, ATPases, and a variety of ATP-requiring enzymes in the cell. The protein reversibly catalyzes the transfer of "energy-rich" phosphate between ATP and creatine or between phospho-creatine (PCr) and ADP. Besides, Fusion (FUS) has been identified as an interactor of CKB, thus a binding ELISA assay was conducted to detect the interaction of recombinant human CKB and recombinant human FUS. Briefly, CKB were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to FUS-coated microtiter wells and incubated for 2h at 37°C. Wells were washed with PBST and incubated for 1h with anti-CKB pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times.With the addition of substrate solution, wells were incubated 15-25 minutes at 37°C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of CKB and FUS was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Figure. The binding activity of C1qA with CRP.The complement component 1q (C1q) is composed of 18 polypeptide chains: six A-chains, six B-chains, and six C-chains. Complement Component 1, Q Subcomponent A (C1qA) is six A-chains of C1q. Complement component 1q (C1q is a protein complex involved in the complement system, which is part of the innate immune system. C1q together with C1r and C1s form the C1 complex. It is potentially multivalent for attachment to the complement fixation sites of immunoglobulin. The sites are on the CH2 domain of IgG and, it is thought, on the CH4 domain of IgM. IgG4 cannot bind C1q, but the other three IgG types can. Besides, C Reactive Protein (CRP) has been identified as an interactor of C1qA, thus a binding ELISA assay was conducted to detect the interaction of recombinant human C1qA and recombinant human CRP. Briefly, C1qA were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100muL were then transferred to CRP-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-C1qA pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of C1qA and CRP was shown in Figure 1, and this effect was in a dose dependent manner.)
WB (Western Blot) (Figure 3. Western Blot Sample: Recombinant DHODH, Human; Antibody: Rabbit Anti-Human DHODH Ab)
SDS-PAGE (Figure 2. SDS-PAGESample: Active recombinant DHODH, Human)
Bioactivity (Dihydroorotate dehydrogenase (DHODH) is an enzyme which catalyzes the fourth enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate, in de novo pyrimidine biosynthesis. This protein is a mitochondrial protein located on the outer surface of the inner mitochondrial membrane. As an enzyme associated with the electron transport chain, DHODH could link mitochondrial bioenergetics, cell proliferation, ROS production, and apoptosis in certain cell types. DHODH depletion also resulted in increased ROS production, decreased membrane potential and cell growth retardation. Besides, FK506 Binding Protein 8 (FKBP8) has been identified as an interactor of DHODH, thus a binding ELISA assay was conducted to detect the interaction of recombinant human DHODH and recombinant human FKBP8. Briefly, DHODH were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to FKBP8-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti- DHODH pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of DHODH and FKBP8 was shown in Figure 1, and this effect was in a dose dependent manner.Figure 1. The binding activity of DHODH with FKBP8)
Bioactivity (Figure. The binding activity of WNT5A with WIF1.Wingless Type MMTV Integration Site Family, Member 5A (WNT5A) is a ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Besides, WNT Inhibitory Factor 1 (WIF1) has been identified as an interactor of WNT5A, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat WNT5A and recombinant rat WIF1. Briefly, WNT5A were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to WIF1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-WNT5A pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of WNT5A and WIF1 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Figure. The binding activity of IGFBP3 with EGFR.Insulin-like growth factor-binding protein 3, also known as IGFBP3 is one of six IGF binding proteins (IGFBP1 to IGFBP6) that have highly conserved structures and bind the insulin-like growth factors IGF-1 and IGF-2 with high affinity. Within tissues, IGFBP3 can bind IGF1 and IGF2 released by many cell types, and block their access to the IGF-1 receptor (IGF1R), which is activated by both IGFs. IGFBP3 also interacts with cell-surface proteins, affecting cell signaling from outside the cell or after internalization, and also enters the cell nucleus where it binds to nuclear hormone receptors and other ligands. Besides, Epidermal Growth Factor Receptor (EGFR) has been identified as an interactor of IGFBP3, thus a binding ELISA assay was conducted to detect the interaction of recombinant human IGFBP3 and recombinant human EGFR. Briefly, IGFBP3 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to EGFR-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-IGFBP3 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of IGFBP3 and EGFR was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (High Mobility Group Protein 1 (HMG1), also known as high mobility group box 1 proteinbelongs to high mobility group and contains HMG-box domain. HMG1 is one of the most important chromatin proteins. This nuclear protein organizes the DNA and regulates transcription. It supports transcription of many genes in interactions with many transcription factors. HMGB1 is secreted by immune cells (like macrophages, monocytes and dendritic cells) through leaderless secretory pathway. Activated macrophages and monocytes secrete HMGB1 as a cytokine mediator of Inflammation. Besides, Tumor Protein p53 (TP53) has been identified as an interactor of HMG1, thus a binding ELISA assay was conducted to detect the interaction of recombinant human HMG1 and recombinant human TP53. Briefly, HMG1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to TP53-coated microtiter wells and incubated for 2h at 37°C. Wells were washed with PBST and incubated for 1h with anti-HMG1 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37°C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of HMG1 and TP53 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Figure. The binding activity of FGF2 with CASP1.Basic fibroblast growth factor (FGF2), also known as bFGF, FGF-beta is a member of a large family of structurally related heparin-binding proteins (the FGFs) involved in the regulation of cell proliferation, growth and differentiation. It involved in many biological processes including angiogenesis, embryonic development and wound healing. Additionally, FGF2 is a critical component of human embryonic stem cell culture medium. Besides, Caspase 1 (CASP1) has been identified as an interactor of FGF2, thus a binding ELISA assay was conducted to detect the interaction of recombinant bovine FGF2 and recombinant bovine CASP1. Briefly, FGF2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to CASP1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FGF2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of FGF2 and CASP1 was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Calmodulin (CAM) is the archetype of the family of calcium-modulated (calmodulin) proteins of which nearly 20 members have been found. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters. Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Besides, Myosin IC (MYO1C) has been identified as an interactor of CAM, thus a binding ELISA assay was conducted to detect the interaction of recombinant human CAM and recombinant human MYO1C. Briefly, CAM were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to MYO1C-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CAMpAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of CAM and MYO1C was shown in Figure 1, and this effect was in a dose dependent manner.Figure 1. The binding activity of CAM with MYO1C)
Bioactivity (Lactoferrin (LF), also known as lactotransferrin (LTF), is a multifunctional protein of the transferrin family. Lactoferrin is one of the components of the immune system of the body; it has antimicrobial activity (bacteriocide, fungicide) and is part of the innate defense, mainly at mucoses. In particular, lactoferrin provides antibacterial activity to human infants. Lactoferrin interacts with DNA and RNA, polysaccharides and heparin, and shows some of its biological functions in complexes with these ligands. LTF is known to activate immune cells to produce several cytokines, such as tumor necrosis factor TNF-a, thus, a stimulation assay was conducted to detect the activity of LTF using human monocytic cell line THP-1. Briefly, THP-1 cells were seeded into wells of 24-well plates at a density of 5×106 cells/mL in RPMI-1640 with the addition of various concentrations of recombinant human LTF. After incubation for 20 hours, the concentration of TNF-a in the cell supernatant was detected using an ELISA kit. TNF-a levels in the cell supernatant of spleen cells increased significantly after stimulated with LTF, the data was shown in table 1.)
Bioactivity (Cluster Of Differentiation 26 (CD26), also known as adenosine deaminase complexing protein 2 or cluster of differentiation 26 (CD26), is a protein in humans. CD26 is an antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. Besides, Eosinophil Chemotactic Factor (ECF) has been identified as an interactor of CD26, thus a binding ELISA assay was conducted to detect the interaction of recombinant human CD26 and recombinant human ECF. Briefly, CD26 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to ECF-coated microtiter wells and incubated for 2h at 37?. Wells were washed with PBST and incubated for 1h with anti- CD26 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of CD26 and ECF was shown in Figure 1, and this effect was in a dose dependent manner.Figure 1. The binding activity of CD26 with ECF(ng/ml).)
Activity (Figure 1. The chemotactic effect of EDN1 on THP1 cells. (A) THP-1 cells were seeded into the upper chambers and serum free RPMI 1640 with 80ng/mL EDN1 was added in lower chamber, then cells in lower chamber were observed at low magnification (•100) after incubation for 3h; (B) THP-1 cells were seeded into the upper chambers and serum free RPMI 1640 without EDN1 was added in lower chamber, then cells in lower chamber were observed at low magnification (•100) after incubation for 3h.)
Activity (FGF23 (Fibroblast growth factor 23) is a member of the fibroblast growth factor family, which possess broad mitogenic and cell survival activities and are involved in a variety of biological processes. A proliferation assay was conducted to detect the bioactivity of recombinant mouse FGF23 using 3T3 cells. Briefly, 3T3 cells were seeded into triplicate wells of 96-well plates at a density of 2,000 cells/well and allowed to attach overnight, then the medium was replaced with serum-free standard DMEM prior to the addition of various concentrations of FGF23. After incubated for 48h, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10uL of CCK-8 solution was added to each well of the plate, then the absorbance at 450nm was measured using a microplate reader after incubating the plate for 1-4 hours at 37 degree C. Proliferation of 3T3 cells after incubation with FGF23 for 48h observed by inverted microscope was shown in Figure 1. Cell viability was assessed by CCK-8 (Cell Counting Kit-8 ) assay after incubation with recombinant FGF23 for 48h. The result was shown in Figure 2. It was obvious that FGF23 significantly increased cell viability of 3T3 cells.)
SDS_PAGE (SDS-PAGE Sample: Active recombinant TNFRSF12A, Human)
Gene Sequencing (Gene Sequencing (extract))
Gene Sequence
Activity (TNFRSF12A (Tumor necrosis factor receptor superfamily member 12A) belongs to the Tumor necrosis factor receptor superfamily. TNFRSF12A is thought to induce apoptosis weakly in some cell types and promotes angiogenesis and the proliferation of endothelial cells. A binding ELISA assay was conducted to detect the association of TNFRSF12A with TNFa. Briefly, TNFRSF12A were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL TNFRSF12A were then transferred to TNFa-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-TNFRSF12A pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of TNFRSF12A and TNFa was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (5'-Nucleotidase, Ecto (NT5E), also known as ecto-5'-nucleotidase or CD73, is an enzyme catalyzing thehydrolysis of nucleoside-5'-monophosphates to nucleosides and inorganic phosphate. The enzyme is a dimer composed of 2 identical 70kD subunits bound by a glycosyl phosphatidyl inositol linkage to the external face of the plasma membrane. NT5E is a marker of lymphocyte differentiation that has functions independent of its catalytic activity, such as T-cell activation and cell-cell adhesion. Other forms of 5-prime nucleotidase exist in the cytoplasm and lysosomes and can be distinguished from NT5E by their substrate affinities, requirement for divalent magnesium ion, activation by ATP, and inhibition by inorganic phosphate. The enzyme is widely distributed in human and animal tissues. Besides, AF4/FMR2 Family, Member 1 (AFF1) has been identified as an interactor of NT5E thus a binding ELISA assay was conducted to detect the interaction of recombinant human NT5E and recombinant human AFF1. Briefly, NT5E were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to AFF1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-NT5E pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of NT5E and AFF1 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Caspase 1 (CASP1) cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. It also has lots of other function, such as defenses against pathogens, cleaves and activates sterol regulatory element binding proteins (SREBPs), promotes apoptosis. Besides, Interleukin 1 Alpha (IL1a) has been identified as an interactor of CASP1, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat CASP1 and recombinant rat IL1a. Briefly, CASP1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to IL1a-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CASP1 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of CASP1 and IL1a was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Golgi Protein 73 (GP73) also known as Golgi phosphoprotein 2 or Golgi membrane protein GP73 is a protein that encoded by the GOLM1 gene. The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. It has been observed to be upregulated in response to viral infection. Besides, Dymeclin (DYM) has been identified as an interactor of GP73, thus a binding ELISA assay was conducted to detect the interaction of recombinant mouse GP73 and recombinant human DYM. Briefly, GP73 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to DYM-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-GP73 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of GP73 and DYM was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Suppressor of cytokine signaling 3 (SOCS3) is a member of the STAT-induced STAT inhibitor (SSI), also known as suppressor of cytokine signaling (SOCS), family that negatively regulates cytokine signal transduction. SOCS3 is feedback inhibitors of the Janus kinase (JAK) and signal transducer and activator of transcription (STAT) signaling pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. SOCS3 also can bind to JAK2 kinase inhibits its kinase activity and nhibits insulin signaling in adipose tissue and the liver. Besides, Glycoprotein 130 (gp130) has been identified as an interactor of SOCS3, thus a binding ELISA assay was conducted to detect the interaction of recombinant mouse SOCS3 and recombinant mouse gp130. Briefly, SOCS3 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to SOCS3-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-SOCS3 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of SOCS3 and gp130 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (The main role of factor VII (FVII) is to initiate the process of coagulation in conjunction with tissue factor (TF). Tissue factor is found on the outside of blood vessels-normally not exposed to the bloodstream. Upon vessel injury, tissue factor is exposed to the blood and circulating FVII. Once bound to TF, FVII is activated to FVIIa by different proteases, among which are thrombin (factor IIa), factor Xa, IXa, XIIa, and the FVIIa-TF complex itself. Tissue Factor (TF) has been identified as an interactor of FVII, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat FVII and recombinant rat TF. Briefly, FVII were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to TF-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FVII pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of FVII and TF was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Calpain 1, Large Subunit (CAPN1) is an intracellular protease that requires calcium for its catalytic activity. Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. It has broad endopeptidase specificity. Besides, Signal Transducer And Activator Of Transcription 3 (STAT3) has been identified as an interactor of CAPN1, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat CAPN1 and recombinant rat STAT3. Briefly, CAPN1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to STAT3-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-CAPN1 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of CAPN1 and STAT3 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Adenine Phosphoribosyltransferase (APRT) is an enzyme involved in the purine nucleotide salvage pathway. It functions as a catalyst in the reaction between adenine and phosphoribosyl pyrophosphate (PRPP) to form AMP. Besides, Vascular Cell Adhesion Molecule 1 (VCAM1) has been identified as an interactor of APRT, thus a binding ELISA assay was conducted to detect the interaction of recombinant human APRT and recombinant human VCAM1. Briefly, APRT were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to VCAM1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-APRT pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of APRT and VCAM1 was shown in Figure 1, and this effect was in a dose dependent manner.)
SDS_PAGE (SDS-PAGE Sample: Active recombinant MDM2, Human)
Application Data (Gene Sequence (extract))
Bioactivity (Mouse double minute 2 homolog (MDM2) also known as E3 ubiquitin-protein ligase Mdm2 is a cellular oncoprotein that recognizes the N-terminal trans-activation domain (TAD) of the p53 tumor suppressor and as an inhibitor of p53 transcriptional activation. The human homologue of this protein is sometimes called Hdm2. The p53 tumor suppressor is the key target of MDM2. It has been identified as a p53 interacting protein that represses p53 transcriptional activity and also acts as an E3 ubiquitin ligase, targeting both itself and p53 for degradation by the proteasome. MDM2 is capable of auto-polyubiquitination, and in complex with p300, a cooperating E3 ubiquitin ligase, is capable of polyubiquitinating p53. Besides, S100 Calcium Binding Protein (S100) has been identified as an interactor of MDM2, thus a binding ELISA assay was conducted to detect the interaction of recombinant human MDM2 and recombinant human S100. Briefly, MDM2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to S100-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-MDM2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of MDM2 and S100 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Regenerating Islet Derived Protein 3 Beta (REG3b) also known as PAP-I and HIP is bactericidal C-type lectin which acts against several intestinal Gram-positive bacteria and Gram-negative bacteria. The Reg family proteins have been implicated in a range of physiological processes including acting as acute phase reactants, lectins, survival/growth factors for insulin-producing pancreatic beta-cells, neural cells, and epithelial cells of the digestive system. To test the effect of REG3b on cell proliferation of SK-N-SH, SK-N-SH cells were seeded into triplicate wells of 96-well plates at a density of 5,000 cells/well and allowed to attach overnight, then the medium was replaced with serum-free standard DMEM prior to the addition of various concentrations of REG3b. After incubated for 72h, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10uL of CCK-8 solution was added to each well of the plate, then measure the absorbance at 450nm using a microplate reader after incubating the plate for 1-4 hours at 37 degree C .Cell proliferation of SK-N-SH cells after incubation with REG3b for 72h observed by inverted microscope was shown in Figure 1.)
SDS_PAGE (SDS-PAGESample: Active recombinant SEMA3A, Human)
Gene Sequencing (Gene Sequencing (extract))
Bioactivity (The Semaphorin 3A (SEMA3A) which belongs to the semaphorin family can function as either a chemorepulsive agent, inhibiting axonal outgrowth, or as a chemoattractive agent, stimulating the growth of apical dendrites. In both cases, the protein is vital for normal neuronal pattern development. Semaphorin 3A is secreted protein containing a Sema domain, an immunoglobulin C2-like domain and a basic domain near the carboxyl tail. It can be secreted by neurons and surrounding tissue to guide migrating cells and axons in the developing nervous system. Besides, Neuropilin 1 (NRP1) has been identified as an interactor of SEMA3A, thus a binding ELISA assay was conducted to detect the interaction of recombinant human SEMA3A and recombinant human NRP1. Briefly, SEMA3A were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to NRP1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-SEMA3A pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of SEMA3A and NRP1 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (Wingless Type MMTV Integration Site Family, Member 5A (WNT5A) is a ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Besides, WNT Inhibitory Factor 1 (WIF1) has been identified as an interactor of WNT5A, thus a binding ELISA assay was conducted to detect the interaction of recombinant mouse WNT5A and recombinant rat WIF1. Briefly, WNT5A were diluted serially in PBS, with 0.01%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to WIF1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-WNT5A pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of of WNT5A and WIF1 was shown in Figure 1, and this effect was in a dose dependent manner.)
Activity (IL17D (Interleukin-17D) belongs to the IL17 (interleukin 17) family, which includes six members (IL-17, IL-17B through IL-17F). IL17D is reported to induce the expression of IL6, CXCL8/IL8, and CSF2/GM-CSF from endothelial cells. IL17 family members share some similarities in AA sequence and structure, thus, a binding ELISA assay was constructed to detect the association of recombinant human IL17D with recombinant human IL17RB. Briefly, IL17D were diluted serially in PBS with 0.1%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to IL17RB-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-IL17D pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of IL17D with IL17RB was shown in Figure 1 and this effect was in a dose dependent manner.)
SDS_PAGE (Sample: Active recombinant IL1RA, Human)
Gene Sequencing (Gene Sequencing (extract))
Bioactivity (IL1RA (interleukin-1 receptor antagonist) is an agent that binds to the cell surface interleukin-1 receptor (IL-1R), which would prevent IL-1 from intracellular signal transduction. Thus, a binding ELISA assay was constructed to detect the association of recombinant human IL1RA with recombinant human IL1R1. Briefly, IL1RA were diluted serially in PBS with 0.1% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to IL1R1-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-IL1RA pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of IL1RA with IL1R1 was shown in Figure 1 and this effect was in a dose dependent manner.)
Bioactivity (IL1RA (interleukin-1 receptor antagonist) is an agent that binds to the cell surface interleukin-1 receptor (IL-1R), which would prevent IL-1 from intracellular signal transduction. Besides, mouse IL1R1 and rat IL1R1 share similarities in amino acid sequence with the identity of 85.6%. Thus, a binding ELISA assay was constructed to detect the association of recombinant mouse IL1RA with recombinant rat IL1R1. Briefly, IL1RA were diluted serially in PBS with 0.1% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to IL1R1-coated microtiter wells and incubated for 2h at 37°C. Wells were washed with PBST and incubated for 1h with anti-IL1RA pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37°C. Finally, add 50AL stop solution to the wells and read at 450nm immediately. The binding activity of IL1RA with IL1R1 was shown in Figure 1 and this effect was in a dose dependent manner.Figure 1. The binding activity of IL1RA with IL1R1.)
ELISA (TGF-beta1 (Transforming growth factor beta 1) is a multifunctional set of peptides that controls proliferation, differentiation, and other functions in many cell types. TGF beta 1 has been shown to interact with TGF beta receptor 1, Decorin, LTBP1 and so on. Thus we have conducted a binding ELISA assay to detect the interaction of recombinant human TGF-Beta1 with recombinant human LTBP1. Briefly, TGF-Beta1 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to LTBP1"coated microtiter wells and incubated for 2h at 37°C. Wells were washed with PBST and incubated for 1h with anti"LTBP1 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15"25 minutes at 37°C. Finally, add 50BL stop solution to the wells and read at 450nm immediately. The binding activity of TGF-Beta1 with LTBP1 was shown in Figure 1 and this effect was in a dose dependent manner.Figure 1. The binding activity of TGF-Beta1 with LTBP1.)
Activity (IL1R1 (Interleukin 1 Receptor Type I), also known as CD121a, is an important mediator involved in many cytokine induced immune and inflammatory responses. It belongs to the interleukin-1 receptor family, and is a receptor for interleukin 1 alpha (IL1A), interleukin 1 beta (IL1B), and interleukin 1 receptor antagonist (IL1RA). Besides, mouse IL1B shares 87.0% AA sequence identity with rat IL1B, suggesting the exist of cross-species activity. Thus, a binding ELISA assay was constructed to detect the association of recombinant rat IL1R1 with recombinant mouse IL1B. Briefly, IL1R1 were diluted serially in PBS with 0.1%BSA (pH 7.4). Duplicate samples of 100uL were then transferred to IL1B-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-IL1R1 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37 degree C. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of IL1R1 with IL1B was shown in Figure 1 and this effect was in a dose dependent manner.)
Activity (Epidermal growth factor (EGF) is a growth factor that stimulates cell growth, proliferation, and differentiation by binding to its receptor EGFR. To test the effect of EGF on cell proliferation of 3T3 fibroblasts, 3T3 cells were seeded into triplicate wells of 96-well plates at a density of 2, 000cells/well and allowed to attach overnight, then the medium was replaced with serum-free standard DMEM prior to the addition of various concentrations of EGF. After incubated for 72h, cells were observed by inverted microscope and cell proliferation was measured by Cell Counting Kit-8 (CCK-8). Briefly, 10uL of CCK-8 solution was added to each well of the plate, then measure the absorbance at 450nm using a microplate reader after incubating the plate for 1-4 hours at 37 degree C .Cell proliferation of 3T3 cells after incubation with EGF for 72h observed by inverted microscope was shown in Figure 1.)
Bioactivity (Figure. The binding activity of LTF with CLU.Lactotransferrin (LTF), also known as actoferrin (LF), is a multifunctional protein of the transferrin family. Lactoferrin belongs to the innate immune system. Apart from its main biological function, namely binding and transport of iron ions, lactoferrin also has antibacterial, antiviral, antiparasitic, catalytic, anti-cancer, and anti-allergic functions and properties. LTF is widely represented in various secretory fluids, such as milk, saliva, tears, and nasal secretions. It also present in secondary granules of PMN and is secreted by some acinar cells. Besides, Clusterin (CLU) has been identified as an interactor of LTF, thus a binding ELISA assay was conducted to detect the interaction of recombinant goat LTF and recombinant goat CLU. Briefly, LTF were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to CLU-coated microtiter wells and incubated for 2h at 37. Wells were washed with PBST and incubated for 1h with anti-LTF pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37. Finally, add 50uL stop solution to the wells and read at 450nm immediately. The binding activity of LTF and CLU was shown in Figure 1, and this effect was in a dose dependent manner.)
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.
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