Rabbit anti-Human HLA-DRB3 Polyclonal Antibody | anti-HLA-DRB3 antibody

Anti-HLA-DRB3 Antibody

Cat. Num. AAA419724

• Gene Names: HLA-DRB3; HLA-DR1B; HLA-DR3B
• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry
• Purity: Affinity Purification
• Synonyms: HLA-DRB3; Polyclonal Antibody; Anti-HLA-DRB3 Antibody; anti-HLA-DRB3 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Western blot analysis of extracts of HepG2 cell lines, using HLA-DRB3 antibody.
• Purity/Purification: Affinity Purification
• Form/Format: Liquid
• Concentration: 1mg/ml (varies by lot)
• Sequence Length: 226

• Applicable Applications for anti-HLA-DRB3 antibody: Western Blot (WB), Immunohistochemistry (IHC)
• Application Notes: WB: 1:500 - 1:2000; IHC: 1:50- 1:200
• Immunogen: Recombinant protein of human HLA-DRB3
• Storage Buffer: PBS with 0.02% sodium azide,50% glycerol, pH7.3.
• Preparation and Storage: Store at -20 degree C (regular) and -80 degree C (long term). Avoid freeze / thaw cycles.

Western Blot (WB)

Related Product Information for anti-HLA-DRB3 antibody

HLA-DRB3 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DRA) and a beta (DRB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues DRB3, DRB4 and DRB5. The presence of DRB3 is linked with allelic variants of DRB1, otherwise it is omitted. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9.

NCBI and Uniprot Product Information

• NCBI GI #: 619534071
• NCBI GeneID: 3125
• Molecular Weight: 29,822 Da
• NCBI Official Full Name: HLA-DRB3, partial
• NCBI Official Synonym Full Names: major histocompatibility complex, class II, DR beta 3
• NCBI Official Symbol: HLA-DRB3
• NCBI Official Synonym Symbols: HLA-DR1B; HLA-DR3B
• NCBI Protein Information: major histocompatibility complex, class II, DR beta 3
• UniProt Protein Name: HLA class II histocompatibility antigen, DRB1-7 beta chain
• Protein Family: HLA class II histocompatibility antigen
• UniProt Gene Name: HLA-DRB1
• UniProt Synonym Gene Names: DR-7; DR7

NCBI Description

HLA-DRB3 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DRA) and a beta (DRB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues DRB3, DRB4 and DRB5. The presence of DRB3 is linked with allelic variants of DRB1, otherwise it is omitted. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9. [provided by RefSeq, Jul 2008]

Uniprot Description

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.