The HLA-DQB1/HLA-DQB2 Antibody (PACO02167) is a specialized tool for research involving the HLA-DQB1 and HLA-DQB2 proteins, key components of the human leukocyte antigen (HLA) system responsible for immune response regulation. This antibody, produced using cutting-edge technology, is highly specific and sensitive, making it ideal for use in various immunology studies.HLA-DQB1 and HLA-DQB2 are essential for antigen presentation and recognition by T cells, playing a crucial role in determining immune responses and susceptibility to autoimmune diseases. The PACO02167 Antibody binds specifically to these proteins, allowing for their detection and analysis in different cell types and tissues.
This makes it a valuable tool for researchers studying autoimmune disorders, transplantation immunology, and infectious diseases.By using the HLA-DQB1/HLA-DQB2 Antibody (PACO02167), researchers can gain important insights into the mechanisms underlying immune responses and diseases, ultimately contributing to the development of novel therapeutic approaches and personalized medicine strategies. Unlock the potential of HLA-DQB1 and HLA-DQB2 research with this powerful antibody.
Antibody Name:
HLA-DQB1/HLA-DQB2 Antibody
Antibody SKU:
PACO02167
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA, WB
Recommended Dilutions:
WB:1:500-1:2000
Species Reactivity:
Human
Immunogen:
synthesized peptide derived from the Internal region of human HLA-DQB1/2.
Form:
Liquid
Storage Buffer:
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Purification Method:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Synonyms:
HLA-DQB1; HLA-DQB; HLA class II histocompatibility antigen, DQ beta 1 chain; MHC class II antigen DQB1; HLA-DQB2; HLA-DXB; HLA class II histocompatibility antigen, DQ beta 2 chain
UniProt Protein Function:
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 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 miroenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. Belongs to the MHC class II family.Protein type: Membrane protein, integralChromosomal Location of Human Ortholog: 6p21.3Cellular Component: Golgi membrane; lysosomal membrane; membrane; MHC class II protein complex; plasma membrane; trans-Golgi network membraneMolecular Function: peptide antigen bindingBiological Process: antigen processing and presentation of exogenous peptide antigen via MHC class II; humoral immune response mediated by circulating immunoglobulin; immunoglobulin production during immune response; T cell costimulation; T cell receptor signaling pathwayDisease: Celiac Disease; Creutzfeldt-jakob Disease; Multiple Sclerosis, Susceptibility To
UniProt Protein Details:
NCBI Summary:
HLA-DQB1 belongs to the HLA class II beta chain paralogs. This class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), 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 it contains six exons. Exon 1 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 DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to four different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2011]