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 (FLT-1 Sandwich ELISA using recombinant human soluble FLT-1 as standard . Mouse anti-human FLT-1 #EWI was used as capture antibody, Biotinylated rabbit anti-human FLT-1 was used for detection)
Application Data (Fig. 2: Inhibition of the VEGF165 induced proliferation in HUVECs by soluble VEGFR-1/Flt-1. VEGF165 (10 ng/mL) was preincubated with increasing amounts of sVEGFR-1/Flt-1 for 1h and then added to the cells.)
Application Data (Fig.1 SDS-PAGE analysis of recombinant human soluble VEGFR-1 produced in insect cells. Sample was loaded in 15% SDS-polyacrylamide gel under reducing condition and stained with Coomassie stain)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human EphB4 at 2 ug/ml (100 ul/well) can bind human EphrinB2 with a linear range of 1-25 ng/ml.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human EFNA1-His at 10 ug/ml (100 ul /well) can bind human EPHA1-Fc, The EC50 of human EPHA1-Fc is 10-30 ng/ml.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human ACE2 protein (Fc tag)(10108-H05H) at 2ug/mL (100uL/well) can bind SARS-CoV Spike/S1 Protein (S1 Subunit, His Tag)(40150-V08B1),the EC50 of SARS-CoV Spike/S1 Protein (S1 Subunit, His Tag)(40150-V08B1) is 400-850 ng/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized human ACE2 protein (Fc tag) (10108-H05H) at 2 ug/mL (100 uL/well) can bind SARS-CoV-2 (2019-nCoV) Spike S1+S2 ECD-His (40589-V08B1), the EC50 of SARS-CoV-2 (2019-nCoV) Spike S1+S2 ECD-His (40589-V08B1) is 400-1200 ng/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized mouse PD-L2-his at 10 ug/mL (100 ul/well) can bind mouse PD1-Fc. The EC50 of mouse PD1-Fc is 1.63 ug/mL.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized canine NTRK-His at 10 ug/ml (100 ul/well) can bind biotinylated mouse BDNF, The EC50 of biotinylated mouse BDNF is 0.07-0.17 ug/ml.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized mouse B7-H2 at 1 ug/ml (100 ul/well) can bind human ICOS with a linear range of 40-1000 ng/ml.)
Bioactivity (Pregnancy-associated plasma protein A(PAPPA), also known as pappalysin-1, is a secreted protease whose main substrate is insulin-like growth factor binding proteins. PAPPA's proteolytic function is activated upon collagen binding. It is thought to be involved in local proliferative processes such as wound healing and bone remodeling. Low plasma level of this protein has been suggested as a biochemical marker for pregnancies with aneuploid fetuses (fetuses with an abnormal number of chromosomes). Besides, Plasminogen (Plg) has been identified as an interactor of PAPPA, thus a binding ELISA assay was conducted to detect the interaction of recombinant human PAPPA and recombinant human Plg. Briefly, biotinylated PAPPA were diluted serially in PBS with 0.01% BSA (pH 7.4). Duplicate samples of 100ul were then transferred to Plg-coated microtiter wells and incubated for 1 h at 37 degree C. Wells were washed 3 times with PBST and incubated for 0.5 h at 37 degree C with SA labelled HRP. After incubation with SA labelled HRP, 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 50uL stop solution to the wells and read at 450/630 nm immediately. The binding activity of PAPPA and Plg was shown in Figure 1, and the ED50 for this effect is 0.04936 ug/ml.)
Bioactivity (The classical complement pathway plays a major role in innate immunity against infection. This pathway is triggered by C1, a multimolecular complex composed of the recognition protein C1q and two serine proteases, C1r and C1s. Following the C1q recognition, C1r is autoactivated, and in turn activates C1s, which cleaves C4 and C2, the C1 substrates. Both C1r and C1s activation involve cleavage of a specific Arg-Ile bond, converting single-chain proenzymes into active proteases of disulfide bond-linked chains (A and B). The full-length (amino acid residues 1-707) of mouse C1r was expressed which activity was measured by its ability to cleaves a thioester substrate Z-Lys-SBzl•HCl. The reaction was performed in 50 mM Tris, pH 7.5 (Assay Buffer), initiated by addition 50 uL of various concentrations of C1r (diluted by Assay Buffer) to 50 ul substrate mixture of 0.2mM Z-Lys-SBzl•HCl and 0.2 mM DTNB. The final well serves as a negative control with no C1r, replaced with 50 ul assay buffer. Then read in kinetic mode for 5 minutes at an absorbance of 405 nm. The specific activity of recombinant mouse C1r is > 500 pmol/min/ug.)
Bioactivity (Hyaluronidase (HAase) is a general term for enzymes that can hydrolyze hyaluronic acid. It is an enzyme that can reduce the activity of hyaluronic acid in the body, thereby improving the fluid permeability in tissues. When used in the human body, it can temporarily reduce the viscosity of the intercellular matrix, promote subcutaneous infusion, locally accumulated exudate or blood to accelerate diffusion and facilitate absorption, and is an important drug dispersant. Clinically used as a drug penetrating agent to promote drug absorption, promote local edema or hematoma dissipation after surgery and trauma. Human HAase consists of 435 amino acids which contains a signal peptide of 1-21 amino acids and it shares 74% and 75% amino acid sequence homology with mouse and rat respectively. The activity assay of recombinant human HAase was measured by its ability to hydrolyze the substrate hyaluronic acid. The rhHAase was diluted to 0.5 ug/ml in 8.46 mM NaH2PO4, 11.54 mM Na2HPO4, 77 mM NaCl, 0.1 mg/ml BSA, pH 7. 50 ul 0.5 ug/ml rhHAase was added into the microplate and start the reaction by adding 50 uL of 0.3 mg/ml substrate which was diluted in 300mM NaH2PO4, pH 5.35. Incubated at 37 degree C for 5min and add 50 ul reaction mixture to 250 ul 1 mg/ml BSA in 24 mM sodium acetic, 79 mM acetic acid, pH 3.75. Incubated at room temperature for 10min and read at a wavelength of 600 nm. The specific activity of recombinant human HAase is >30 pmol/min/ug.)
Bioactivity (Complement Component 9 (C9), a component of the Membrane attack Complex (MAC) plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. During MAC assembly, multiple copies of C9 are sequentially recruited to membrane associated C5b8 to form a pore. Thus a functional binding ELISA assay was conducted to detect the interaction of recombinant human C9 and recombinant human C5. Briefly, biotin-linked C9 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 ul were then transferred to C5-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 C9 and recombinant human C5 was shown in Figure 1, the EC50 for this effect is 0.13 ug/mL.)
Bioactivity (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 rat 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 rat TFPI (MW: 61.9 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 rat TFPI significantly decreased trypsin activity. The inhibition IC50 was )
Bioactivity (Figure 2. The hemagglutination assay of GAL4 in V- bottom shaped 96-well microtiter plate.)
Bioactivity (Galectin-4(GAL4) is a protein that in humans is encoded by the LGALS4 gene. The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. LGALS4 is an S-type lectin that is strongly undere)
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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