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 (Inhibition of the basic FGF-induced proliferation of HUVE cells by recombinant human sFGFR-1-Fc. HUVECs were stimulated with 10 ng/ml bFGF, the soluble receptor was added with a 50 - 200X excess)
SDS-PAGE (SDS-PAGE analysis of recombinant human soluble FGFR-1/Fc produced in insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.)
ELISA (SARS COV2 S B.1.1.529 trimer ACE functional binding ELISA assay2019-ncov S B.1.1.529 trimer(coating at 0.1ug-well) binding with Human ACE2-Fc.The linear range was found to be 23 ng/ml)
Tris-Bis-PAGE (S B.1.1.529 trimer protein PAGE1ug loaded Tris-Bis PAGE under reducing condition. The purity is greater than 95%.)
Application Data (Polarized membrane extensions mediate osteoclast fusion.(D, top) Immunoblot analysis of lysates of RAW264.7 macrophages stimulated with RANKL for the indicated times with antibodies to Ser473-phosphorylated (p) or total forms of Akt.)
Application Data (In vitro differentiation of human osteoclasts and confocal microscope analysisHuman osteoclasts were generated by culture of peripheral blood monocytes with M-CSF and RANKL using a standard protocol.Peripheral blood mononuclear cells (PBMCs) were isolated from heparinized blood samples by Ficoll density gradient centrifugation.PBMCs were cultured either on glass coverslips for differentiation analysis or on dentine discs for resorption assays in alpha MEM , 10% FCS , 1% Ultraglutamine , 1% Pen/Strep, 25 ng/mL human M-CSF , and 30 ng/mlankl (ocky , , ).Cells were cultured for 2 weeks with medium changes twice weekly.Cells on coverslips were fixed in 4% paraformaldehyde (PFA) in 1× phosphate-buffered saline (PBS) and then stained with Phalloidin-Alexa 488 , DAPI , and tartrate-resistant acid phosphatase (TRAP) activity using Naphtol-AS-MX-Phosphate and Fast-Red-Violet LB .TRAP-positive cells with ?3 nuclei and actin rings were counted as osteoclasts.Dentine discs were cleaned with 1% SDS and resorption pits were visualized by black…)
Application Data ((A) Nitrite production by HT-29 cells following 48 h of treatment with cytokines.Effect of 0–50 ng/ml TNF-? on nitrite production induced by 100 U/ml IFN-? and 10 ng/ml IL-1? in HT-29 cells following 48 h of treatment.)
Application Data (Replicative control of HCV in JFH-1/Huh7.5.1 system with conditioned media (CM) from pU/UC-transfected pDC-GEN2.2 cells.E) Recombinant Type III Interferons in the absence of CM at the same concentrations as found in the CM (IL-28A/IFN?2: 1500 pg/mL; IL-28B/IFN?3: 10 pg/mL; IL-29/IFN?1: 500 pg/mL) were added to JFH-1 infected Huh7.5.1 cells.)
Application Data (Effects of ACM from Olig2PC-Astros and NPC-Astros on neurons.(h and i) RT-PCR analysis of the expression of the antioxidant defense-related genes, GCLC and NFE2L2 (n=3), and the neurotrophic growth factor genes, BDNF, GDNF and NT-3 (n=3).)
Application Data (Alterations of gene expression of neurotrophins in the DRG after HSV-1 infection.Gene expression levels of ATF3 and neurotrophins (NGF, GDNF, BDNF, and NT3) were normalized to the GAPDH level, and are presented as the fold change in the ratio of the affected side to the contralateral one.)
Application Data (The SCG SC development assay is free of GDNF.Western Blot for GDNF with different dilutions of rat-tail collagen (20?l, 10?l, 5?l, 2.5?l, 1.25?l and 0.6125?l collagen) were analyzed using anti-GDNF antibody specific for human and rat GDNF.)
Bioactivity (The activity was determined by immobilized Spike Protein S1 binding with human ACE2 in a functional ELISA assay, the ED50 was determined to be 3.8nM.2019-ncov S1-his tagged (coating at 0.5ug-well) binding with Human ACE2-Fc (cat. The linear range was found to be 0.1-5 ug/ml)
SDS-PAGE (The recombinant S1-His protein migrates as 120kDa due to glycosylation)
Application Data (Fig. 2: Dose-dependent stimulation of cell proliferation in NFS60 cells by recombinant human M-CSF. Values are the means (±SD) of triplicate determinations and expressed as percentage of control.)
SDS-PAGE (Fig. 1: SDS-PAGE analysis of recombinant human M-CSF. Samples were loaded in 18% SDS-polyacrylamide gel under reducing and non-reducing conditions and stained with Coomassie blue.)
ELISA (Figure 2.Functional ELISA: Recombinant human PlGF-2 was coated with 0.5ug/ml and increasing amounts of recombinant human sFlt-1(5) was added as standard . The monoclonal mouse anti-human VEGFR1/Flt-1 antibody in combination with a goat anti-mouse Biotin antibody was used for detection.)
BioLISA (Fig 2: Binding of sEGFRto recombinant human EGF in a functional ELISA. EGF [AAA79134] was coated with 200ng/well to a 96-well plate and sEGFR was added with increasing concentrations up to 4000ng/ml. Detection was performed using a polyclonal rabbit anti-human EGFR [] (1 ug/ml, 100 ul/well) and a goat anti-rabbit Biotin conjugated secondary antibody.)
SDS-PAGE (Fig. 1: SDS-PAGE analysis of recombinant human soluble EGFR from insect cells. Sample was loaded in 10% SDS-polyacrylamide gel under reducing conditions and stained with Coomassie Blue.)
SDS-PAGE (SDS-PAGESample: Active recombinant FGF18, Human)
Bioactivity (Fibroblast Growth Factor-18 (FGF18) is a trophic factor for mature chondrocytes and their progenitors. It has been reported to have significant anabolic effects on cartilage. FGF18 plays a central role in skeletal growth and development.Besides, Ly1 Antibody Reactive Homolog (LYAR) has been identified as an interactor of FGF18, thus a binding ELISA assay was conducted to detect the interaction of recombinant human FGF18 and recombinant human LYAR. Briefly, FGF18 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100ul were then transferred to LYAR-coated microtiter wells and incubated for 2h at 37 degree C. Wells were washed with PBST and incubated for 1h with anti-FGF18 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 FGF18 and LYAR was shown in Figure 1, and this effect was in a dose dependent manner.)
Bioactivity (Figure 2. Cell proliferation of TF-1 cells after stimulated with IL4.)
Bioactivity (The interleukin 4 (IL4,) is a cytokine that induces differentiation of naive helper T cells (Th0 cells) to Th2 cells. Upon activation by IL4, Th2 cells subsequently produce additional IL4 in a positive feedback loop. IL4 has many biological roles, includi)
Bioactivity (HTRF assay for NEK2 activity 1 uM STK S3 substrate was incubated with different concentrations of NEK2 protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, and 100 uM ATP for 1 hour. Then 10 ul detection reagents containing anti-STK antibody (1:2) and SA-XL665 (1:100) diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Bioactivity (HTRF assay for NEK2 activity 1 uM STK S3 substrate was incubated with different concentrations of NEK2 protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, and 100 uM ATP for 1 hour. Then 10 ul detection reagents containing anti-STK antibody (1:2) and SA-XL665 (1:100) diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Application Data (Measured by its binding ability in a functional ELISA. Immobilized mouse EphA6 at 1 ug/ml (100 ul/well) can bind human EphrinA3 / Fc Chimera. The EC50 of human EphrinA3 is 299.2 ng/mL.)
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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