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Recombinant Human HLA class II histocompatibility antigen, DQ alpha 2 chain(HLA-DQA2),partial

SKU : BHP10502069

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CUSABIO TECHONOLOGY LLC

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Mfr.No.	CSB-RP148294h
Alternative Names	DX alpha chainHLA class II histocompatibility antigen, DQ(6) alpha chainHLA-DQA1MHC class II DQA2
Tag	N-terminal 6xHis-tagged
Regulatory	RUO
Relevance	Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents th 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 mbrane 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 syst 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 roval 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 mbrane 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.
Source	E.coli
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Expression Region	24-214aa
Mol Weight	25.6kDa
Nature	recombinant
Protein Description	Partial

Subcellular Location	Cell membrane, Single-pass type I membrane protein, Endoplasmic reticulum membrane, Single-pass type I membrane protein, Golgi apparatus, trans-Golgi network membrane, Single-pass type I membrane protein, Endosome membrane, Single-pass type I membrane protein, Lysosome membrane, Single-pass type I membrane protein
Uniprot	P01906, P01906
Database Links	HGNC:4943 OMIM:613503 KEGG:hsa:3118 STRING:9606.ENSP00000364076 UniGene:Hs.591798
Function	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.
Pathway	Antigen processing and presentation; Hematopoietic cell lineage; Th1 and Th2 cell differentiation; Th17 cell differentiation
Protein Families	MHC class II family
Research Area	Immunology
Tissue Specificity	Restricted to skin Langerhans cells, although some expression at low levels may occur at the surface of B lymphoblastoid cells.
Weight	25.7kDa

Stotage Note	Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Buffer	Tris-based buffer，50% glycerol
Purity	Greater than 90% as determined by SDS-PAGE.
Storage	The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Buffer	Tris-based buffer,50% glycerol

Immunogen Species	Homo Sapiens (Human)

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SKU	Supplier No.	Size	Your price	Quantity
BHP10502069	CSB-RP148294h	1mg	$1812		Add to Cart
BHP10502069	CSB-RP148294h	100ug	$419		Add to Cart
BHP10502069	CSB-RP148294h	20ug	$224		Add to Cart

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