At AAA Biotech, we offer a comprehensive selection of high-quality recombinant proteins for use in a wide range of research areas, including immunology, neuroscience, stem cell research, cancer research and more. No matter whether you need recombinant proteins for cell expansion, polarization, differentiation, or cell processing applications, we have got you covered.
Our recombinant proteins undergo rigorous quality testing. So, you can rely on AAA Biotech for high-quality recombinant proteins to support your research. Explore our catalog to find the right protein for your research needs.
Standard Curve (Sample) (The titer has been suggested in reference to an "in-house" ELISA kit performed at Rekom Biotech over the first lot obtained.Each end user should carry out their own titration for their particular application.Figure 2. In this plot, the optical density at 450/620 nm for positive (blue) and negative (gray) IgM sera are compared for each concentration of the recombinant antigen. An appropriate statistical test of significance for the comparison of means between both groups, the Welch's test, is employed. Eligible concentrations for the use of the antigen should present statistically significant differences between positive and negative sera. This happens when the intervals at the top do not overlap and, equivalently, when the pvalue at the bottom is below 0.05. In the present figure, all p-values are below 0.05 and thus the intervals do not overlap. Therefore, any of the showed concentrations can be used to distinguish between positive and negative sera.)
WB (Western Blot) (Recombinant SUV420H1 (2-387) activity assay 2 ug Recombinant Nucleosomes (H3.1) were incubated with 0 ug (-), 0.2 ug (+), 0.4 ug (++), 0.8 ug (+++) SUV420H1 (2-387) protein, respectively, in 30 ul reaction system containing 50 mM Tris-HCl, pH 8.6, 0.02% Triton X-100, 2 mM MgCl2, 1 mM TCEP, 50 uM SAM for 3 hr at room temperature. 6 ul reaction products were loaded and run on a 12.5% SDS-PAGE gel. Western Blot was used to detect the generation of reaction products (H4K20me3 antibody). SUV420H1 (2-387) only was used as negative control. The Western blot result shows that nucleosomes are much better than histone octamers as the substrate of SUV420H1 (2-387).)
SDS-PAGE (Recombinant SUV420H1 (2-387) protein gel. 10% SDS-PAGE gel stained with Coomassie blue. MW: 71.1 kDa Purity: > 75% )
WB (Western Blot) (Recombinant p300 protein, catalytic domain activity assay 0.5 ug of histone H4 were incubated with 0, 50, 100, 200 ng of p300, catalytic domain respectively in 20 ?l reaction system including 50 mM Tris-HCl pH 8.6, 0.02% Triton X-100, 2 mM MgCl2, 1 mM TCEP and 20 ?M acetyl- CoA for 2 hr at room temperature. For each reaction, 10 ?l of product was run on a 12.5% SDS-PAGE gel and detected by Western Blot. H4 pan-acetyl antibody was used to recognize acetylated histone H4.)
SDS-PAGE (Recombinant p300 protein, catalytic domain, protein gel 10% SDS-PAGE Coomassie staining MW: 98.7 kDa Purity: > 90% )
Application Data (HTRF for YTHDF2 (401-554) activity 3 uM oligo m6A ssDNA (GTTGG/m6A/CTT) was incubated with different concentrations of YTHDF2 (401-554) protein in 10 ul reaction system containing 50 mM HEPES-NaOH pH 7.5, 0.1% BSA for 1 hour, then 10 ul DYKDDDDK antibody and SA-XL665 mixture (1:100 dilution in the same buffer) was added to each reaction system and incubated for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Application Data (HTRF for YTHDF2 (401-554) activity 3 uM oligo m6A ssDNA (GTTGG/m6A/CTT) was incubated with different concentrations of YTHDF2 (401-554) protein in 10 ul reaction system containing 50 mM HEPES-NaOH pH 7.5, 0.1% BSA for 1 hour, then 10 ul DYKDDDDK antibody and SA-XL665 mixture (1:100 dilution in the same buffer) was added to each reaction system and incubated for 30 min. All the operations and reactions were performed at room temperature. HTRF assay was used for detection.)
Application Data (HTRF Assay for Recombinant BRD2 (344-455) activity. 3 uM histone peptide H4K5/8/12/16(4Ac) was incubated with BRD2 (344-455) protein in reaction buffer including 50mM HEPES-NaOH pH 7.0, 0.1% BSA for 1 hour at room temperature. Anti-DYKDDDDK antibody was used to detect reaction products.)
Application Data (HTRF Assay for Recombinant BRD2 (344-455) activity. 3 uM histone peptide H4K5/8/12/16(4Ac) was incubated with BRD2 (344-455) protein in reaction buffer including 50mM HEPES-NaOH pH 7.0, 0.1% BSA for 1 hour at room temperature. Anti-DYKDDDDK antibody was used to detect reaction products.)
SDS-PAGE (Recombinant BRD2 (344-455) protein gel. BRD2 (344-455) protein was run on a 12% SDS-PAGE gel and stained with Coomassie Blue.MW:19.4 kDa )
Application Data (Recombinant PBRM1 (613-734) HTRF activity assay. 3 uM histone peptide H4K5/8/12/16(4Ac) was incubated with PBRM1 (613-734) protein in reaction buffer including 50mM HEPES-NaOH pH 7.0 and 0.1% BSA for 1 hour at room temperature. Anti-DYKDDDDK antibody was used to detect reaction products.)
SDS-PAGE (Recombinant PBRM1 (613-734) protein gel. PBRM1 (613-734) protein was run on a 10% SDS-PAGE gel and stained with Coomassie Blue.)
Application Data (PRC2 EZH2 (A677G) complex activity assay. PRC2 EZH2(A677G) complex activity measured using an HMT assay. MALDI-TOF was used for detection.)
SDS-PAGE (Recombinant PRC2 EZH2 (A677G) complex gel. PRC2 EZH2(A677G) complex was run on an SDS-PAGE gel and stained with Coomassie Blue.)
Application Data (Recombinant DNMT1 protein activity assay Assay was performed using DNMT Activity / Inhibition Assay,. The substrate, AdoMet and DNMT1 were incubated for 1 hour at 37 degree C. The whole reactions were developed for 4 min. )
SDS-PAGE (Recombinant DNMT1 protein gel. Recombinant DNMT1 protein was run on an 8% SDS-PAGE gel and stained with Coomassie blue. MW: 188.2 kDa Purity: > 90%)
Application Data (Recombinant TAF1 (1522-1656) protein activity assay. 3 uM histone peptide H3K18ac peptide was incubated with Recombinant TAF1 (1522-1656) protein in a reaction system containing 50 mM HEPES-NaOH pH 7.4, and 0.1% BSA for 1 hour at room temperature. DYKDDDDK antibody and SA-XL665 (each at 1:100 in reaction buffer) was added for 30 min. All operations were performed at RT. HTRF assay was used for detection of reaction products.)
Application Data (Recombinant TAF1 (1522-1656) protein activity assay. 3 uM histone peptide H3K18ac peptide was incubated with Recombinant TAF1 (1522-1656) protein in a reaction system containing 50 mM HEPES-NaOH pH 7.4, and 0.1% BSA for 1 hour at room temperature. DYKDDDDK antibody and SA-XL665 (each at 1:100 in reaction buffer) was added for 30 min. All operations were performed at RT. HTRF assay was used for detection of reaction products.)
SDS-PAGE (Recombinant TAF1 (1522-1656) protein gel. TAF1 (1522-1656) protein was run on a 12.5% SDS-PAGE gel and stained with Coomassie Blue. MW: 19.3 kDa Purity: ? 90%)
WB (Western Blot) (Recombinant NSD2 (MMSET)-SET activity assay 2 ug recombinant nucleosomes were incubated with NSD2 (MMSET)-SET protein in reaction buffer for 3 hours at room temperature. Western blot was used to detect the generation of reaction products using Histone H3K36me2 antibody. NSD2-SET only was used as negative control.)
SDS-PAGE (Recombinant NSD2 (MMSET)-SET protein gel. Recombinant NSD2 (MMSET)-SET run on a 12.5% SDS-PAGE gel and stained with Coomassie Blue. MW: 60 kDa Purity: > 90%)
Application Data (Recombinant SMYD2 protein activity assay 2 ug Calf Thymus Octamers was incubated with 0.5 ug and 1 ug SMYD2 protein respectivley in reaction buffer containing radioactive 3H-SAM for 3 hours at room temperature. Activity was detected by Autoradiography. *Our result showed that H4 may also be methylated by SMYD2.)
SDS-PAGE (Recombinant SMYD2 protein gel SMYD2 protein was run on an 8% SDS-PAGE gel and stained with Coomassie blue.)
Application Data (MALDI-TOF for JARID1B / KDM5B (2-751) activity. 3.3 uM H3K4me3 (1-21 aa) peptide was incubated with 100 nM or 200 nM JARID1B / KDM5B (2-751) protein in reaction buffer for 2 hours at room temperature. MALDI-TOF was used for detection.Catalytic Ability: > 60 turnovers/ enzyme molecule)
Application Data (HTRF assay for JARID1B /KDM5B (2-751) activity 3 uM H3K4me3 (1-21 aa) peptide was incubated with KDM5B (2-751) protein in reaction buffer for 1 hour at room temperature.Anti-H3K4me2-d2 antibody was used to detect reaction product.)
SDS-PAGE (Recombinant JARID1B / KDM5B (2-751) was run on a 12.5% SDS-PAGE gel and stained with Coomassie Blue. MW: 100 kDaPurity: >80%)
WB (Western Blot) (Western Blot analysis for Mononucleosomes H3K9me3 (EPL) Unmodified mononucleosomes (Lane 1) and Mononucleosomes H3K9me3 (Lane 2) were detected with H3K9me3 antibody and H4 antibody, respectively. H4 was detected as loading control. Only Mononucleosomes H3K9me3 can be detected by H3K9me3 antibody. Nucleosomes = Mononucleosomes)
Application Data (Recombinant Mononucleosomes H3K9me3 (EPL) - DNA gel. Mononucleosomes H3K9me3 (EPL) were run on a 2% agarose gel and stained with ethidium bromide. Lane 1: DNA marker. Lane 2: 601 DNA. Lane 3: Intact mononucleosomes. Intact mononucleosomes migrate much higher than free 601 DNA. The agarose gel result shows almost all of 601 DNA wraps histone octamers to form mononucleosomes. Nucleosomes = Mononucleosomes)
SDS-PAGE (Recombinant Mononucleosomes H3K9me3 (EPL) protein gel. Recombinant Mononucleomes were run on a 12.5% SDS-PAGE gel and stained with Coomassie Blue. Purity: ? 95%)
Application Data (Recombinant IDH2 (R140K) protein activity assay 10 uM NADPH and 1 uM a-KG were incubated with 100 nM IDH2 (R140K) protein in 200 ul reaction system (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 10 mM MgCl2 and 0.03% BSA, room temp). Depletion of NADPH was monitored continuously at Abs 340 nm for 20 min.)
SDS-PAGE (Recombinant IDH2 (R140K) protein gel 12.5% SDS-PAGE Coomassie staining MW: 51.7 kDa Purity: > 95% )
Application Data (Recombinant Human interleukin-11 (AAA50427) was analyzed under reducing denaturing conditions (Lane 2). The molecular weight (kDa) of the marker proteins (Lane 1) are displayed on the left hand of the image. Bands were visualized using Coomassie stains.)
ELISA (Sandwich ELISA analysis of human IL-11 using Mouse anti Human interleukin-11 as a capture reagent and biotinylated Mouse anti Human interleukin-11 as a detection reagent with recombinant Human interleukin-11 (AAA50427) as the antigen.)
Recombinant protein expressed in E Coli and purified by ion exchange chromatography >=90 % determined by coomassie blue staining of a reducing SDS-PAGE gel
Application Data (A microtiter plate was coated overnight with recombinant human VEGF-A at a concentration of 5 ug/ml. After washing and blocking with PBST+5% BSA, 10% human serum was added spiked with increasing concentrations of bevacizumab. Detection was performed using Human Anti-Ranibizumab Antibody, clone AbD29865 (HCA307, cross-reactive with bevacizumab) at a concentration of 2 mug/ml and a rat anti-DYKDDDDK-tag antibody in HISPEC Assay Diluent (BUF049A) followed by QuantaBlu Fluorogenic Peroxidase Substrate. Data are shown as the mean of three measurements.)
Application Data (A microtiter plate was coated overnight with recombinant human VEGF-A at a concentration of 5 ug/ml. After washing and blocking with PBST+5% BSA, 10% human serum was added spiked with increasing concentrations of ranibizumab. Detection was performed using Human Anti-Ranibizumab Antibody, clone AbD29928 (HCA304) at a concentration of 2 ug/ml and a rat anti-DYKDDDDK-tag antibody in HISPEC Assay Diluent (BUF049A) followed by QuantaBlu Fluorogenic Peroxidase Substrate. Data are shown as the mean of three measurements)
Recombinant proteins are purified laboratory reagents produced through genetic engineering. A specific gene of interest is inserted into a host organism, such as mammalian, bacterial, yeast, or insect cells, which then expresses the protein in a controlled environment.
The recombinant process utilized to generate the recombinant proteins in our catalog provides precise control over sequence modifications, expression levels, and large-scale production tailored to experimental needs. These recombinants are widely used in research to investigate protein-protein interactions, enzyme activities, receptor-ligand binding, and cellular responses. Additionally, recombinant proteins serve as standards or controls in immunostaining assays and support cell growth and differentiation in culture systems, particularly in immunology, oncology, and structural biology studies.
Common Applications of Recombinant Proteins
Studying protein-protein and protein-DNA interactions
Functional assays to study biological pathways
Standard curves in ELISA and other quantitative assays
Use as antigens for antibody production
Development and screening of therapeutic drugs
Biomarker discovery and validation
Cell signaling and immune response studies
Vaccine research and development
Key Features of AAA Biotech’s Recombinant Proteins
High Purity: Most proteins are purified to ≥95% using affinity chromatography and other validated techniques.
Biological Activity: If functional activity is tested and confirmed for a given protein, it will be noted directly on the product page.
Multiple Expression Systems: Available in E. coli, HEK293, CHO, yeast, and insect cells to match your assay requirements.
Custom Tags Available: His-tag, GST, FLAG, and Fc fusion options for easy purification and detection.
Wide Range of Targets: Cytokines, growth factors, enzymes, receptors, signaling proteins, and more.
Validated Consistency: Lot-to-lot consistency ensured through rigorous QC protocols.
Flexible Quantities: Available in various pack sizes to suit different experimental needs.
Ready-to-Use Format: Lyophilized or liquid formulations that are easy to reconstitute and use.
Why Buy Recombinant Proteins from AAA Biotech?
At AAA Biotech, we are committed to supporting the research community with recombinant proteins that offer exceptional performance and reliability. Our proteins are produced using industry-standard methods and are validated to meet the needs of academic, pharmaceutical, and biotechnology laboratories.
With competitive pricing, global shipping, and dedicated technical support, AAA Biotech makes it simple and convenient to source the high-quality recombinant proteins your work depends on.
FAQ
1. How are AAA Biotech recombinant proteins validated?
Each batch undergoes stringent quality control checks, including SDS-PAGE analysis, endotoxin testing (for select products), and activity assaying (for select products). Certificates of Analysis are provided with every product.
2. Are your proteins suitable for therapeutic development or only research?
AAA Biotech recombinant proteins are strictly for research-use only and are not intended for diagnostic or therapeutic purposes in humans or animals.
3. What types of expression systems do you use for recombinant protein production?
The production labs use a variety of expression platforms, including bacterial (E. coli), yeast, insect (baculovirus), and mammalian (HEK293, CHO) systems. The expression system used depends on the complexity and intended function/use of the protein.
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.