HLA class II histocompatibility antigen, DP alpha 1 Recombinant Protein | HLA-DPA1 recombinant protein

Recombinant Human HLA class II histocompatibility antigen, DP alpha 1 chain protein

Cat. Num. AAA1265567

• Gene Names: HLA-DPA1; PLT1; HLADP; HLASB; DP(W3); DP(W4); HLA-DP1A
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: HLA class II histocompatibility antigen; DP alpha 1; Recombinant Human HLA class II histocompatibility antigen; DP alpha 1 chain protein; DP(W3); DP(W4); HLA-SB alpha chain; MHC class II DP3-alpha; MHC class II DPA1; HLA-DPA1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 29-222aa; Extracellular Domain
• Sequence: AGAIKADHVSTYAAFVQTHRPTGEFMFEFDEDEMFYVDLDKKETVWHLEEFGQAFSFEAQGGLANIAILNNNLNTLIQRSNHTQATNDPPEVTVFPKEPVELGQPNTLICHIDKFFPPVLNVTWLCNGELVTEGVAESLFLPRTDYSFHKFHYLTFVPSAEDFYDCRVEHWGLDQPLLKHWEAQEPIQMPETTE
• Sequence Length: 260

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for HLA-DPA1 recombinant protein

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 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 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 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.

Product Categories/Family for HLA-DPA1 recombinant protein

Immunology

References

The genomic organisation and nucleotide sequence of the HLA-SB(DP) alpha gene.Lawrance S.K., Das H.K., Pan J., Weissman S.M.Nucleic Acids Res. 13:7515-7528(1985) Class II genes of the human major histocompatibility complex. Evolution of the DP region as deduced from nucleotide sequences of the four genes.Gustafsson K., Widmark E., Jonsson A.-K., Servenius B., Sachs D.H., Larhammar D., Rask L., Peterson P.A.J. Biol. Chem. 262:8778-8786(1987) Epitope recognition by a DP alpha chain-specific monoclonal antibody (DP11.1) is influenced by the interaction between the DP alpha chain and its polymorphic DP beta chain partner.Young J.A., Lindsay J., Bodmer J.G., Trowsdale J.Hum. Immunol. 23:37-44(1988) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.Isotypic and allotypic variation of human class II histocompatibility antigen alpha-chain genes.Auffray C., Lillie J.W., Arnot D., Grossberger D., Kappes D., Strominger J.L.Nature 308:327-333(1984) A novel DPA1 allele (DPA1*0203) composed of known epitopes.Muntau B., Thye T., Pirmez C., Horstmann R.D.Tissue Antigens 49:668-669(1997) Three new DP alleles identified in sub-Saharan Africa DPB1*7401, DPA1*02013, and DPA1*0302.Steiner L.L., Cavalli A., Zimmerman P.A., Boatin B.A., Titanji V.P., Bradley J.E., Lucius R., Nutman T.B., Begovich A.B.Tissue Antigens 51:653-657(1998) Sequencing-based typing reveals new insight in HLA-DPA1 polymorphism.Rozemuller E.H., Bouwens A.G., van Oort E., Versluis L.F., Marsh S.G., Bodmer J.G., Tilanus M.G.Tissue Antigens 45:57-62(1995) A new HLA-DPA1 allele, DPA1*02016, identified in African-American population.McDaniel D.O., Nguyen C., McDaniel L.S.Tissue Antigens 56:197-198(2000) High-resolution sequence-based DPA1 typing identified two novel DPA1 alleles, DPA1*010303 and DPA1*0303, from a Kenyan population.Luo M., Bamforth J., Gill K., Cohen C., Brunham R.C., Plummer F.A.Tissue Antigens 65:120-122(2005) Identification of a novel DPA1 allele, DPA1*010602, in an East African population.Peterson T.A., Luo M., Mao X., Brunham R.C., Plummer F.A.Hum. Immunol. 69:885-886(2008) Description of two novel HLA-DPA1 alleles DPA1*0110 and DPA1*010304.Lee K.W.Tissue Antigens 71:575-577(2008) A novel HLA-DPA1*0204 allele was identified in a Chinese individual.Zhao H., Dai W.-J., He Y.-M., Zhu F.-M., Yan L.-X.Tissue Antigens 71:577-578(2008) Steiner L., Begovich A., Suraj V.One new DPA1 Allele.Grams S.E., Begovich A., Mangaccat J.Novel human HLA-DPA1 allele identified in potential bone marrow donors.Bassinger S., Wu J., Williams T.M.DPA1 polymorphism in Polynesians.Varney M.D., Gavrilidis A., Abbott W.DPA1*0105, a novel DPA1 variant in a negrois population.May J., Krestchmer C., Schnittger L., Striecker R., Kremoner P.G., Meyer C.G.Tissue Antigens 48:593-594(1996) Exon 2, 3, and 4 polymorphism of HLA-DPA1.Rozemuller E.H., Versluis L.F., Bouwens A.G., Tilanus M.G.Immunogenetics 41:53-53(1995) Sequences related to HLA-DR alpha chain on human chromosome 6 restriction enzyme polymorphism detected with DC alpha chain probes.Trowsdale J., Lee J., Carey J., Grosveld F., Bodmer J., Bodmer W.Proc. Natl. Acad. Sci. U.S.A. 80:1972-1976(1983) Invariant chain structure and MHC class II function.Cresswell P.Cell 84:505-507(1996) Presentation of antigens by MHC class II molecules getting the most out of them.Villadangos J.A.Mol. Immunol. 38:329-346(2001) MHC class II molecules on the move for successful antigen presentation.Rocha N., Neefjes J.EMBO J. 27:1-5(2008) Autophagy in MHC class II presentation sampling from within.Menendez-Benito V., Neefjes J.Immunity 26:1-3(2007) MHC class II transport at a glance.Berger A.C., Roche P.A.J. Cell Sci. 122:1-4(2009) CD74 in antigen presentation, inflammation, and cancers of the gastrointestinal tract.Beswick E.J., Reyes V.E.World J. Gastroenterol. 15:2855-2861(2009) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 335883185
• NCBI GeneID: 3113
• NCBI Accession #: NP_001229453.1
• NCBI GenBank Nucleotide #: NM_001242524.1
• UniProt Accession #: P20036; O19722; O46883; P01905; P79554; Q2Q060; Q2Q061; Q5EY03; Q5STP1; Q6DQK4; A9YWH7; B9UKH4
• Molecular Weight: 26.3 kDa
• NCBI Official Full Name: HLA class II histocompatibility antigen, DP alpha 1 chain
• NCBI Official Synonym Full Names: major histocompatibility complex, class II, DP alpha 1
• NCBI Official Symbol: HLA-DPA1
• NCBI Official Synonym Symbols: PLT1; HLADP; HLASB; DP(W3); DP(W4); HLA-DP1A
• NCBI Protein Information: HLA class II histocompatibility antigen, DP alpha 1 chain
• UniProt Protein Name: HLA class II histocompatibility antigen, DP alpha 1 chain
• Protein Family: HLA class II histocompatibility antigen
• UniProt Gene Name: HLA-DPA1
• UniProt Synonym Gene Names: HLA-DP1A; HLASB
• UniProt Entry Name: DPA1_HUMAN

NCBI Description

HLA-DPA1 belongs to the HLA class II alpha chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DPA) and a beta (DPB) chain, 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 and its gene contains 5 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DP molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules. [provided by RefSeq, Jul 2008]

Uniprot Description

HLA-DPA1: 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, integral

Chromosomal Location of Human Ortholog: 6p21.3

Cellular Component: cell surface; endosome membrane; Golgi membrane; integral to plasma membrane; lysosomal membrane; MHC class II protein complex; plasma membrane; trans-Golgi network membrane

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

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