HLA-DQA1, Polyclonal Antibody

HLA class II histocompatibility antigen; DQ alpha 1 chain; DC-1 alpha chain; DC-alpha; HLA-DCA; MHC class II DQA1; HLA-DQA1

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit Ig

Rabbit

This HLA-DQA1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 188-222 amino acids from the C-terminal region of human HLA-DQA1.

Purified Rabbit Polyclonal Antibody (Pab)

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Vial Concentration: 0.5 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-HLA-DQA1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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.

Crown Antibodies; Immunology; Neuroscience

Western Blot (WB), ELISA (EIA)

WB~~1:2000

All lanes : Anti-HLA-DQA1 Antibody (C-term) at 1:8000 dilution
Lane 1: Daudi whole cell lysates
Lane 2: Raji whole cell lysates

Lysates/proteins at 20 ug per lane.

Secondary
Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution

Predicted band size : 28 kDa

Blocking/Dilution buffer: 5% NFDM/TBST.

Anti-HLA-DQA1 Antibody (C-term)at 1:2000 dilution + human spleen lysates

Lysates/proteins at 20 ug per lane.

Secondary
Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution

Predicted band size : 28 kDa

Blocking/Dilution buffer: 5% NFDM/TBST.

27805

major histocompatibility complex, class II, DQ alpha 1

HLA class II histocompatibility antigen, DQ alpha 1 chain

HLA class II histocompatibility antigen, DQ alpha 1 chain

DQA1_HUMAN

HLA-DQA1 belongs to the HLA class II alpha chain paralogues. The 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 alpha chain is approximately 33-35 kDa. It is encoded by 5 exons; exon 1 encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, and exon 4 encodes the transmembrane domain and 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. [provided by RefSeq, Jul 2008]

HLA-DQA1 iso4:

Protein type: Cell surface; Membrane protein, integral

Chromosomal Location of Human Ortholog: 6p21.3

Cellular Component: Golgi membrane; membrane; lysosomal membrane; integral to plasma membrane; plasma membrane; trans-Golgi network membrane; endosome membrane; MHC class II protein complex; external side of plasma membrane

Molecular Function: MHC class II receptor activity; peptide antigen binding

Biological Process: positive regulation of T cell differentiation; cytokine and chemokine mediated signaling pathway; T cell costimulation; antigen processing and presentation of exogenous peptide antigen via MHC class II; immune response; T cell receptor signaling pathway

Chang H.-C.,et al.Nature 305:813-815(1983).
Schenning L.,et al.EMBO J. 3:447-452(1984).
Auffray C.,et al.Nature 308:327-333(1984).
Schiffenbauer J.,et al.J. Immunol. 139:228-233(1987).
Ellis M.C.,et al.Immunogenetics 46:410-417(1997).

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