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 (Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 10-40 ng/mL in the presence of 10 ng/mL recombinant Activin A.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized mouse CD105 at 10 ug/ml (100 ul/well) can bind human TGFRB1 with a linear ranger of 6.4-800 ng/ml.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized recombinant human Angiopoietin-2 at 10 ug/ml (100 ul/well) can bind Human Tie2 / Fc chimera with a range of 0.2-20 ug/ml.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human ANGPT2 at 10 ug/ml (100 ul /well) can bind human Tie2-Fch, The EC50 of human Tie2-Fch is 0.1-0.3ug/ml.)
Bioactivity (Interleukin 10 (IL10), also known as human cytokine synthesis inhibitory factor (CSIF), is an anti-inflammatory cytokine. IL10 is a cytokine with multiple, pleiotropic, effects in immunoregulation and inflammation. It downregulates the expression of Th1 cytokines, MHC class II antigens, and co-stimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL10 can block NF-B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Investigation also has shown that IL-10 predominantly inhibits lipopolysaccharide (LPS) and bacterial product mediated induction of the pro-inflammatory cytokines TNF, IL-1, IL-12 and IFN secretion from Toll-Like Receptor (TLR) triggered myeloid lineage cells. Besides, Interleukin 10 Receptor Alpha (IL10Ra) has been identified as an interactor of IL10, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat IL10 and recombinant rat IL10Ra. Briefly, IL10 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to IL10Ra-coated microtiter wells and incubated for 2h at 37. Wells were washed with PBST and incubated for 1h with anti-IL10 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 IL10 and IL10Ra was shown in Figure 1, and this effect was in a dose dependent manner.Figure. The binding activity of IL10 with IL10Ra.)
Bioactivity (Complement factor B (CFB), a 95-kDa protein, is a crucial catalytic element of the alternative pathway (AP) of complement. After binding of CFB to C3b, activation of the AP depends on the proteolytic cleavage of CFB by factor D to generate the C3 converta)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized TNFRSF18-His at 10 ug/mL (100 uL/well) can bind TNFSF18-mFc, the EC50 of TNFSF18-mFc is 20-60 ng/mL.)
Application Data (Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is typically 0.015-0.06 ug/mL.)
Application Data (Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation. The ED50 for this effect is typically 20-60 ng/mL in the presence of 10 ng/mL recombinant Activin A.)
Bioactivity (Aprotinin (AP) is a competitive serine protease inhibitor. Reversibly binds to and blocks the enzymatic active site. Inhibits a range of serine proteases including trypsin, chymotrypsin, kallikrein and plasmin. Inhibits cytopathogenic effect of SARS-CoV-2 and double-stranded RNA formation in SARS-CoV-2-infected cells. The activity of recombinant bovine AP was measured by its ability to inhibit trypsin cleavage of a peptide substrate BAPNA in the assay buffer 200 mM Triethanolamine hydrochloride, 20 mM CaCl2, pH 7.8. The reaction was performed in adding 20 ul 4 mg/mL trypsin diluted by 1mM HCl to 160 ul assay buffer and 20 ul 0.85% (w/v) NaCl and start the reaction by adding 100 ul of 1mg/ml BAPNA. Include a substrate blank containing 160 ul assay buffer, 20 ul 1mM HCl, 20 ul 0.85% (w/v) NaCl and 100 uL of 1mg/ml substrate. Rapidly mixing at 25 degree C, then read at 405 nm in kinetic mode for 5 minutes using a microplate reader controlling the ?A405nm/min=0.08-0.12. The 20 ul different concentrations of recombinant bovine AP was incubated with 20 ul 4 mg/mL trypsin in 160 ul assay buffer at 25 degree C for 10 minutes followed by adding 100 ul substrate, then read at 405 nm in kinetic mode for 5 minutes using a microplate reader. Under these conditions, the enzyme amount of 50% inhibition of trypsin activity per minute is defined as a unit. The specific activity of recombinant bovine AP is >2000 U/mg.)
Greater than 95.0% as determined by: (a)Analysis by RP-HPLC. (b)Analysis 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.
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