HLA-DRA Antibody (Clone # 302CT2.3.2)
Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P01903 |
Host | Mouse |
Clonality | Monoclonal |
Isotype | Mouse IgM |
Clone Names | Clone # 302CT2.3.2 |
Calculated MW | 28621 Da |
Gene ID | 3122 |
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Positive Control | Western blot: ZR-75-1 cell lysate. |
Application & Usage | WB: 1:500 – 1:16000. |
Other Names | HLA-DRA; HLA-DRA1; HLA class II histocompatibility antigen, DR alpha chain; MHC class II antigen DRA |
Target/Specificity | HLA-DRA |
Antibody Form | Liquid |
Appearance | Colorless liquid |
Formulation | Crude ascites with 0.09% (W/V) sodium azide. |
Handling | The antibody solution should be gently mixed before use. |
Reconstitution & Storage | -20 °C |
Background Descriptions | |
Precautions | HLA-DRA Antibody (Clone # 302CT2.3.2) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | HLA-DRA |
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Synonyms | HLA-DRA1 |
Function | An alpha chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the beta chain HLA- DRB, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DR-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 (PubMed:29884618, PubMed:17334368, PubMed:8145819, PubMed:15322540, PubMed:22327072, PubMed:27591323, PubMed:31495665, PubMed:15265931, PubMed:9075930, PubMed:24190431). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). 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 (PubMed:31495665). 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 (PubMed:17182262, PubMed:23783831). 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 (PubMed:25413013). 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 (PubMed:8145819). |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Autolysosome membrane; Single-pass type I membrane protein. Note=The MHCII complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation (PubMed:9075930, PubMed:18305173). Component of immunological synapses at the interface between T cell and APC (PubMed:15322540, PubMed:29884618). |
Tissue Location | Expressed in professional APCs: macrophages, dendritic cells and B cells (at protein level) (PubMed:31495665, PubMed:15322540, PubMed:23783831). Expressed in thymic epithelial cells (at protein level) (PubMed:23783831). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Major histocompatibility complex (MHC) class II molecules destined for presentation to CD4+ helper T cells is determined by two key events. These events include the dissociation of class II-associated invariant chain peptides (CLIP) from an antigen binding groove in MHC II å/∫ dimers through the activity of MHC molecules HLA-DM and -DO, and subsequent peptide antigen binding. Accumulating in endosomal/lysosomal compartments and on the surface of B cells, HLA-DM, -DO molecules regulate the dissociation of CLIP and the subsequent binding of exogenous peptides to HLA class II molecules (HLA-DR, -DQ and -DP) by sustaining a conformation that favors peptide exchange. RFLP analysis of HLA-DM genes from rheumatoid arthritis (RA) patients suggests that certain polymorphisms are genetic factors for RA susceptibility. HLA-B belongs to the HLA class I heavy chain paralogs. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. HLA-B and -C can form heterodimers consisting of a membrane anchored heavy chain and a light chain (∫-2-Microglobulin). Polymorphisms yield hundreds of HLA-B and -C alleles.
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