{"product_id":"recombinant-human-hla-class-ii-histocompatibility-antigen-drb1-beta-chain-hla-drb1-partial-bhp10511753","title":"Recombinant Human HLA class II histocompatibility antigen, DRB1 beta chain (HLA-DRB1), partial","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eRecombinant Human HLA class II histocompatibility antigen, DRB1 beta chain (HLA-DRB1), partial is a recombinant protein preparation from Homo sapiens (Human) designed for use in assay development, binding studies, and functional characterization. Key attributes such as expression system, expressed region, and affinity tag(s) help researchers match the reagent to specific experimental readouts.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E.coli expression is commonly used for rapid, scalable production. For targets that require glycosylation or other post-translational modifications, consider how a prokaryotic system may affect folding or activity.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e The expressed fragment (30-227aa) focuses the reagent on a defined domain\/segment, which can influence binding interfaces and epitope availability.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s)\/format:\u003c\/strong\u003e His\/Myc tags can support purification and detection in pull-down or binding assays; confirm that the tag position does not interfere with the interaction of interest.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e ≥90% (SDS-PAGE) provides a quick checkpoint for reagent quality in downstream analytical workflows.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Supplied as Liquid or Lyophilized powder; select the format that best fits your lab’s handling and aliquoting preferences.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eRecombinant design choices (expression host, fragment boundaries, and tag configuration) help balance yield, solubility, and assay compatibility. Choose conditions and controls that match the recombinant format to your experimental question.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHLA-DRB1\u003c\/strong\u003e has been reported to be involved in A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells. Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes. In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins. Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance. The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut\/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens\/self-peptides. The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules. ; Allele DRB1*01:01: Displays an immunodominant epitope derived from Bacillus anthracis pagA\/protective antigen, PA (KLPLYISNPNYKVNVYAVT), to both naive and PA-specific memory CD4-positive T cells. Presents immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (PHQFINLRSNNSATLIVPYV), contributing to viral clearance. Displays commonly recognized peptides derived from IAV external protein HA (PKYVKQNTLKLAT and SNGNFIAPEYAYKIVK) and from internal proteins M, NP and PB1, with M-derived epitope (GLIYNRMGAVTTEV) being the most immunogenic. Presents a self-peptide derived from COL4A3 (GWISLWKGFSF) to TCR (TRAV14 biased) on CD4-positive, FOXP3-positive regulatory T cells and mediates immune tolerance to self. May present peptides derived from oncofetal trophoblast glycoprotein TPBG 5T4, known to be recognized by both T-helper 1 and regulatory T cells. Displays with low affinity a self-peptide derived from MBP (VHFFKNIVTPRTP). ; Allele DRB1*03:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance. Displays self-peptides derived from retinal SAG (NRERRGIALDGKIKHE) and thyroid TG (LSSVVVDPSIRHFDV). Presents viral epitopes derived from HHV-6B gH\/U48 and U85 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection. Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and long-term protection. ; Allele DRB1*04:01: Presents an immunodominant bacterial epitope derived from M. tuberculosis esxB\/culture filtrate antigen CFP-10 (EISTNIRQAGVQYSR), eliciting CD4-positive T cell effector functions such as IFNG production and cytotoxic activity. May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance. Presents tumor epitopes derived from melanoma-associated TYR antigen (QNILLSNAPLGPQFP and DYSYLQDSDPDSFQD), triggering CD4-positive T cell effector functions such as GMCSF production. Displays preferentially citrullinated self-peptides derived from VIM (GVYATR\/citSSAVR and SAVRAR\/citSSVPGVR) and ACAN (VVLLVATEGR\/ CitVRVNSAYQDK). Displays self-peptides derived from COL2A1. ; Allele DRB1*04:02: Displays native or citrullinated self-peptides derived from VIM. ; Allele DRB1*04:04: May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (HIVMQYMYVPPGAPIPTTRN) and VP2 (RGDSTITSQDVANAVVGYGV), contributing to viral clearance. Displays preferentially citrullinated self-peptides derived from VIM (SAVRAR\/citSSVPGVR). ; Allele DRB1*04:05: May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. ; Allele DRB1*05:01: Presents an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. ; Allele DRB1*07:01: Upon EBV infection, presents latent antigen EBNA2 peptide (PRSPTVFYNIPPMPLPPSQL) to CD4-positive T cells, driving oligoclonal expansion and selection of a dominant virus-specific memory T cell subset with cytotoxic potential to directly eliminate virus-infected B cells. May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (VPYVNAVPMDSMVRHNNWSL), contributing to viral clearance. In the context of tumor immunesurveillance, may present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (MTEYKLVVVGAVGVGKSALTIQLI), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. In metastatic epithelial tumors, presents to intratumoral CD4-positive T cells a KRAS neoantigen (MTEYKLVVVGAVGVGKSALTIQLI) carrying G12V hotspot driver mutation and may mediate tumor regression. ; Allele DRB1*11:01: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SDRIIQITRGDSTITSQDVA), contributing to viral clearance. Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and longterm protection. In the context of tumor immunesurveillance, may present tumor-derived neoantigens to CD4-positive T cells and trigger anti-tumor helper functions. ; Allele DRB1*13:01: Presents viral epitopes derived from HHV-6B antigens to polyfunctional CD4-positive T cells implicated in control of HHV-6B infection. ; Allele DRB1*15:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SNNSATLIVPYVNAVPMDSM), contributing to viral clearance. Displays a self-peptide derived from MBP (ENPVVHFFKNIVTPR). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. ; Allele DRB1*15:02: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. ; (Microbial infection) Acts as a receptor for Epstein-Barr virus on lymphocytes.. When interpreting results, consider species context, domain architecture, and whether the recombinant format represents full-length or a defined region.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eAntigen and virulence-factor studies that compare strain- or domain-specific binding and immune recognition.\u003c\/li\u003e\n\u003cli\u003eUse of recombinant proteins as standards for quantitative assays and serology-oriented method development.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eBinding and interaction assays:\u003c\/strong\u003e quantify partner binding and rank conditions using plate-based formats or biophysical methods (SPR\/BLI).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCell-based functional studies:\u003c\/strong\u003e evaluate dose–response and time-course effects in relevant cell systems when the target acts extracellularly or through receptor engagement.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay development:\u003c\/strong\u003e use as a standard, spike-in control, or positive control where consistent specifications are required.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpretation typically relies on relative comparisons (treated vs control, mutant vs wild-type, or dose\/time series) using consistent sample handling and appropriate normalization.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePost-translational modifications:\u003c\/strong\u003e expression system can affect glycosylation and processing; interpret differences cautiously when comparing to native protein.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIsoforms and domains:\u003c\/strong\u003e expressed regions may not capture all isoform-specific features; match fragment boundaries to your assay’s binding site.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eControls:\u003c\/strong\u003e include blank matrix controls, tag-only controls (where relevant), and orthogonal readouts (e.g., WB\/qPCR\/ELISA) to support interpretation.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProt Knowledgebase entry for HLA-DRB1 — UniProt — https:\/\/www.uniprot.org\/ - NCBI Gene for HLA-DRB1 — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - RCSB Protein Data Bank — RCSB PDB — https:\/\/www.rcsb.org\/ - PubMed (reviews and primary literature) — NCBI — https:\/\/pubmed.ncbi.nlm.nih.gov\/ - Ensembl gene summary — Ensembl — https:\/\/www.ensembl.org\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53058996633965,"sku":"CSB-EP355781HU-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53059101786477,"sku":"CSB-EP355781HU-100UG","price":578.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53059101819245,"sku":"CSB-EP355781HU-20UG","price":306.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP355781HU-SDS.jpg?v=1772271091","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-hla-class-ii-histocompatibility-antigen-drb1-beta-chain-hla-drb1-partial-bhp10511753","provider":"BioHippo","version":"1.0","type":"link"}