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HLA-DRB1

Major histocompatibility complex, class II, DR beta 1

Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.

Gene Name: Major histocompatibility complex, class II, DR beta 1
Synonyms: HLA-DRB1, DRB1, HLA-DR1B, HLA-DRB, Human leucocyte antigen DRB1, MHC class II antigen DRB1*10, MHC class II antigen, MHC class II antigen DRB1*1, HLA-DRB2, Lymphocyte antigen DRB1, SS1
Target Sequences: NM_002124 NP_002115.2 P01911

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HLA-DRB1 Protein - (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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E. coli
10His-SUMO, N-terminus + Myc, C-terminus
1 mg/$1,355; 100 µg/$420; 20 µg/$323
HLA-DRB1 Protein - Recombinant Major Histocompatibility Complex Class II DR Beta 1 By SDS-PAGE
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E. coli
His, N-Terminal
30.7 kDa
10 µg/$286; 50 µg/$472; 100 µg/$752; 200 µg/$942; 1 mg/$2,069; 500 µg/$1,600; 5 mg/$3,291; 2 mg/$2,257
HLA-DRB1 Protein
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E. coli
His
100 µg/$361; 500 µg/$739; 20 µg/$261
HLA-DRB1 Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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293T Cells
Myc-DDK (Flag)
29.97 kDa
20 µg/$150
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HEK 293 Cells
6His, N-terminus
23 kDa
100 µg/$298
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HEK 293 Cells
6His, N-terminus
23 kDa
200 µl/$283
HLA-DRB1 Protein
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E. coli
His, N-Terminal
23 kDa
10 µg/$265; 200 µg/$484; 50 µg/$315
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HEK 293 Cells
Myc-DDK (Flag)
27 kDa
20 µg/$1,107
HLA-DRB1 Protein - Recombinant Major Histocompatibility Complex Class II DR Beta 1 By SDS-PAGE
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E. coli
His-T7
31.1 kDa
10 µg/$286; 50 µg/$472; 100 µg/$752; 200 µg/$942; 1 mg/$2,069; 500 µg/$1,600; 5 mg/$3,291; 2 mg/$2,257
HLA-DRB1 Protein
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E. coli
His
31.2 kD
1 mg/$1,355; 100 µg/$420; 20 µg/$323
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For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).