AAA Biotech 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.
Application Data (WNT3 Is a Functional Biomarker for Predicting the DE Differentiation Potential (A) WNT3 levels in control and various knockdown HUES8 sublines correlate with their DE differentiation efficiency.The four protocols included the following treatments in a serum-free medium: (1) A - > A (Activin A only for 4 days); (2) AW - > A (Activin A and Wnt3a for 2 days followed by Activin A only for another 2 days); (3) A - > AX (Activin A only for 2 days followed by Activin A and XAV 939 for another 2 days); and (4) AW - > AX (Activin A and Wnt3a for 2 days followed by Activin A and XAV 939 for another 2 days).)
Application Data (Differentiation from human iPS cells toward hepatic lineage cells.Human iPS cells were sequentially stimulated with various cytokines: (1) activin A, (2) basic FGF and BMP-4, and (3) HGF.)
Application Data (K02288 selectively inhibits BMP signaling.)
Application Data (Loss of REX1 within the pluripotent population primes cells for differentiation.n?=?3 E) Fold enrichment of the percentage of GATA4 positive endoderm cells generated from TRA+VEN? cells relative to those from TRA+VEN+ population after 3 days of treatment with Activin A and BMP4 in low serum media, as observed by immunocytochemistry.)
Application Data (Directed differentiation of hESC-derived cysts to RPE using transwell filters.Ac+/Ac?: with or without Activin A.)
Application Data (Fig. 3: Confluent PAE/KDR cells were stimulated with 50ng/ml human VEGF165 for 10 min at 37°C. Cells were lysed and an IP was performed using a mouse anti-human KDR antibody (Cat# WB was performed with a mouse anti-human KDR antibody (Cat# and an anti- Phosphotyrosine antibody.)
Bioactivity (Multimerin 1 (MMRN1) is a secreted glycoprotein that consists of multiple subunits, forming a complex with a molecular weight of approximately 150 kDa. MMRN1 is a member of the multimerin family and it is mainly expressed in platelets and endothelial cells. MMRN1 plays an important role in maintaining vascular integrity, regulating clotting and inflammatory responses, among others. In addition, the binding of MMRN1 to Vitronectin (VTN) plays an important role in a variety of physiological and pathological processes, including cell adhesion, migration, blood coagulation, and cell signaling. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human MMRN1 and recombinant human VTN. Briefly, MMRN1 was diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to VTN-coated microtiter wells and incubated for 1h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-MMRN1 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 MMRN1 and recombinant human VTN was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Figure 2. Cell proliferation of M-NFS-60 cells after stimulated with G-CSF.)
Bioactivity (G-CSF is a pleiotropic cytokine best known for its specific effects on the proliferation, differentiation, and activation of hematopoietic cells of the neutrophilic granulocyte lineage. It is produced mainly by monocytes and macrophages upon activation by endotoxin, TNF-alpha and IFN-gamma. In addition, various carcinoma cell lines and myeloblastic leukemia cells can express G-CSF constitutively. In vitro, G-CSF stimulates growth, differentiation and functions of cells from the neutrophil lineage. Consistent with its in vitro functions, G-CSF has been found to play important roles in defense against infection, in inflammation and repair, and in the maintenance of steady state hematopoiesis. The activity of G-CSF is usually measured by a cell proliferation assay using M-NFS60 mouse myelogenous leukemia lymphoblast cells. M-NFS60 cells were seeded into triplicate wells of 96-well plates at a density of 8,000 cells/well with 2% serum standard 1640 which contains various concentrations of recombinant pig G-CSF. After incubated for 3 days, 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 the absorbance at 450 nm was measured using a microplate reader after incubating the plate for 2-4 hours at 37 degree C. Proliferation of M-NFS-60 cells after incubation with G-CSF for 3 days 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 pig G-CSF for 3 days. The result was shown in Figure 2. It was obvious that G-CSF significantly increased cell viability of M-NFS-60 cells. The EC50 is 0.3 ng/ml)
Bioactivity (Figure. The binding activity of FGF23 with FGFR2.Fibroblast growth factor 23 or FGF23 is a member of the fibroblast growth factor (FGF) family which is responsible for phosphate and vitamin D metabolism. The main function of FGF23 seems to be regulation of phosphate concentration in plasma. FGF23 decreases the reabsorption and increases excretion of phosphate and suppress 1-alpha-hydroxylase, reducing its ability to activate vitamin D and subsequently impairing calcium absorption. Besides, Fibroblast Growth Factor Receptor 2 (FGFR2) has been identified as an interactor of FGF23, thus a binding ELISA assay was conducted to detect the interaction of recombinant human FGF23 and recombinant human FGFR2. Briefly, FGF23 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to FGFR2-coated microtiter wells and incubated for 2h at 37. Wells were washed with PBST and incubated for 1h with anti-FGF23 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 FGF23 and FGFR2 was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Lipoprotein, a (Lpa) is a lipoprotein subclass. Lpa is assembled at the hepatocyte cell membrane surface, while other scenarios exist with regard to the location of assembly. It mainly exists in plasma. Lpa contributes to the process of atherogenesis. It also may enhance coagulation by inhibiting the function of tissue factor pathway inhibitor. Lpa carries cholesterol and binds atherogenic proinflammatory oxidized phospholipids as a preferential carrier of oxidized phospholipids in human plasma, which attract inflammatory cells to vessel walls and leads to smooth muscle cell proliferation. Moreover, Lpa also is hypothesized to be involved in wound healing and tissue repair, interacting with components of the vascular wall and extra cellular matrix. Besides, Fibronectin (FN) has been identified as an interactor of Lpa, thus a binding ELISA assay was conducted to detect the interaction of recombinant human Lpa and recombinant human FN. Briefly, Lpa were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to FN-coated microtiter wells and incubated for 2h at 37?. Wells were washed with PBST and incubated for 1h with anti-Lpa 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 Lpa and FN was shown in Figure 1, and this effect was in a dose dependent manner.)
>90% as determined by SDS-PAGE quantitative densitometry by Coomassie Blue staining.
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.
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