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.
Bioactivity (Tissue inhibitors of metalloproteinases or TIMPs are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four members of the family, TIMP-1, TIMP-2, TIMP-3, and TIMP-4. TIMP-2 is a non N-glycosylated protein with a molecular mass of 22 kDa produced by a wide range of cell types, which inhibits MMPs non-covalently by the formation of binary complexes. TIMP-2 also has erythroidpotentiating and cell growth promoting activities. The activity of recombinant bovine TIMP2 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 rbTIMP2 (MW: 51.75 KD) was diluted to different concentrations with the assay buffer. Mix 8 ul of rhTIMP2 curve dilutions, 12.8 ul of activated rbMMP-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 bovine TIMP2 significantly decreased rhMMP2 activity. The inhibition IC50 was )
Bioactivity (Annexin V (ANXA5) is a multifunctional protein that is highly expressed on the apical surfaces of syncytiotrophoblasts, and plays an important role in haemostatic regulations, maintaining blood fluidity of the placenta. Lower ANXA5 levels have been observ)
Bioactivity (Apolipoprotein A2 (APOA2) is a major protein component of serum HDL. It is produced by the liver and is involved in cholesteryl ester formation and cholesterol transport from tissues to the liver. Polymorphisms of APOA2 are associated with disorders of ch)
Bioactivity (Aspartate transaminase(AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or glutamic oxaloacetic transaminase, is a pyridoxal phosphate-dependent transaminase enzyme AST catalyzes the reversible transfer of an alpha-amino group between aspa)
Bioactivity (Ribonuclease P (RNASEP) is a type of ribonuclease which cleaves RNA. RNase P is unique from other RNases in that it is a ribozyme – a ribonucleic acid that acts as a catalyst in the same way that a protein based enzyme would. Its function is to cleave off an extra, or precursor, sequence of RNA on tRNA molecules. Besides, Methyl CpG Binding Protein 2 (MECP2) has been identified as an interactor of RNASEP, thus a binding ELISA assay was conducted to detect the interaction of recombinant human RNASEP and recombinant human MECP2. Briefly, RNASEP were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100L were then transferred to MECP2-coated microtiter wells and incubated for 2h at 37. Wells were washed with PBST and incubated for 1h with anti-RNASEP 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 RNASEP and MECP2 was shown in Figure 1, and this effect was in a dose dependent manner.Figure. The binding activity of RNASEP with MECP2.)
Bioactivity (Figure. The binding activity of GDNF with GFRa2.Glial cell-derived neurotrophic factor (GDNF) is a small protein that potently promotes the survival of many types of neurons. This protein was shown to promote the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. GDNF is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. Besides, Glial Cell Line Derived Neurotrophic Factor Receptor Alpha 2 (GFRa2) has been identified as an interactor of GDNF, thus a binding ELISA assay was conducted to detect the interaction of recombinant human GDNF and recombinant human GFRa2. Briefly, GDNF were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100uL were then transferred to GFRa2-coated microtiter wells and incubated for 2h at 37. Wells were washed with PBST and incubated for 1h with anti-GDNF 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 GDNF and GFRa2 was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Growth arrest and DNA-damage-inducible protein GADD45 alpha (GADD45a) is a member of the GADD45 family. It may affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase. In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity. Besides, Proliferating Cell Nuclear Antigen (PCNA) has been identified as an interactor of GADD45a, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat GADD45a and recombinant rat PCNA. Briefly, GADD45a were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100L were then transferred to PCNA-coated microtiter wells and incubated for 2h at 37. Wells were washed with PBST and incubated for 1h with anti-GADD45a 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 GADD45a and PCNA was shown in Figure 1, and this effect was in a dose dependent manner.Figure. The binding activity of GADD45a with PCNA.)
WB (Western Blot) (Sample: Active recombinant AST, Human)
SDS_PAGE (SDS-PAGE)
Identification (Gene Sequencing (extract))
Bioactivity (Aspartate transaminase(AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or glutamic oxaloacetic transaminase, is a pyridoxal phosphate-dependent transaminase enzyme AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. In this test, an amino group is transferred of from aspartate to -ketoglutarate. The products of this reversible transamination reaction are oxaloacetate and glutamate. The oxaloacetic acid can be decomposed into pyruvate and carbon dioxide with the present of phenylamine citrate. The activity of aspartate transaminase can be measured by calculating the concentration of the pyruvate. The reaction was performed in adding 10ul different concentation recombinant AST(the blank tube add 10ul phosphate buffer) to 50ul mixture substrate contianing 2mM 2-Ketoglutaric acid, 0.1M L-aspartic acid, in 0.2M phosphate buffer,pH7.4, incubate at 37°C for 1h, then add 10ul phenylamine citrate and 50ul 2,4-dinitrophenylhydrazine continue incubate at 37°C for 20min, stop the action by adding 500ul 0.4M NaOH, read the OD value at 520nm. Standard curve prepare by double dilute 2uM pyruvate with phosphate bufferr then add 10ul phenylamine citrate and 50ul 2,4-dinitrophenylhydrazine, incubate at 37°C for 20min and record the OD value at 520nm. One unit of AST is the amount of enzyme that will generate 1umole of pyruvate per minute at pH7.4 at 37°C.)
SDS-PAGE (SDS-PAGE analysis of recombinant human soluble TIE-2/Fc produced from insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.)
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.
Submit a Question
Please complete the form below and a representative will contact you as soon as possible.
Request more Information
Please complete the form below and a representative will contact you as soon as possible.
Request a Manual
Please complete the form below and a representative will contact you as soon as possible.
Request a Quote
Please complete the form below and a representative will contact you as soon as possible.