This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This HLA-DQB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 13-39 amino acids from the N-terminal region of human HLA-DQB1.
HLA-DQB1
Reactivity: Human
WB
Host: Rabbit
Polyclonal
unconjugated
Application Notes
WB: 1:1000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Expiry Date
6 months
Larhammar, Hyldig-Nielsen, Servenius, Andersson, Rask, Peterson: "Exon-intron organization and complete nucleotide sequence of a human major histocompatibility antigen DC beta gene." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 80, Issue 23, pp. 7313-7, (1984) (PubMed).
Boss, Strominger: "Cloning and sequence analysis of the human major histocompatibility complex gene DC-3 beta." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 81, Issue 16, pp. 5199-203, (1984) (PubMed).
Larhammar, Andersson, Andersson, Bill, Böhme, Claesson, Denaro, Emmoth, Gustafsson, Hammarling: "Molecular analysis of human class II transplantation antigens and their genes." in: Human immunology, Vol. 8, Issue 1, pp. 95-103, (1983) (PubMed).
Larhammar, Schenning, Gustafsson, Wiman, Claesson, Rask, Peterson: "Complete amino acid sequence of an HLA-DR antigen-like beta chain as predicted from the nucleotide sequence: similarities with immunoglobulins and HLA-A, -B, and -C antigens." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 79, Issue 12, pp. 3687-91, (1982) (PubMed).
Target
HLA-DQB1
(Major Histocompatibility Complex, Class II, DQ beta 1 (HLA-DQB1))
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 an 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 miroenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.