Proteasome activator complex subunit 2 Recombinant Protein | PSME2 recombinant protein

Recombinant Human Proteasome activator complex subunit 2

Cat. Num. AAA717237

• Gene Names: PSME2; PA28B; REGbeta; PA28beta
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Proteasome activator complex subunit 2; Recombinant Human Proteasome activator complex subunit 2; 11S regulator complex subunit beta; REG-beta; Activator of multicatalytic protease subunit 2; Proteasome activator 28 subunit beta; PA28b; PA28beta; PSME2 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: 2-239aa; Full Length
• Sequence: AKPCGVRLSGEARKQVEVFRQNLFQEAEEFLYRFLPQKIIYLNQLLQEDSLNVADLTSLRAPLDIPIPDPPPKDDEMETDKQEKKEVHKCGFLPGNEKVLSLLALVKPEVWTLKEKCILVITWIQHLIPKIEDGNDFGVAIQEKVLERVNAVKTKVEAFQTTISKYFSERGDAVAKASKETHVMDYRALVHERDEAAYGELRAMVLDLRAFYAELYHIISSNLEKIVNPKGEEKPSMY
• Sequence Length: 239

• 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 PSME2 recombinant protein

Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.

Product Categories/Family for PSME2 recombinant protein

Cell Biology

References

Organization of the genes encoding the human proteasome activators PA28alpha and beta.McCusker D., Wilson M., Trowsdale J.Immunogenetics 49:438-445(1999) Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome.Ahn J.Y., Tanahashi N., Akiyama K., Hisamatsu H., Noda C., Tanaka K., Chung C.H., Shibmara N., Willy P.J., Mott J.D., Slaughter C.A., De;Martino G.N.FEBS Lett. 366:37-42(1995) The DNA sequence and analysis of human chromosome 14.Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.Nature 421:601-607(2003) Bienvenut W.V.Submitted (OCT-2004) to UniProtKB Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.Biochemistry 46:3553-3565(2007) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) 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)

NCBI and Uniprot Product Information

• NCBI GI #: 30410792
• NCBI GeneID: 5721
• NCBI Accession #: NP_002809.2
• NCBI GenBank Nucleotide #: NM_002818.2
• UniProt Accession #: Q9UL46; Q15129
• Molecular Weight: 54.3 kDa
• NCBI Official Full Name: proteasome activator complex subunit 2
• NCBI Official Synonym Full Names: proteasome activator subunit 2
• NCBI Official Symbol: PSME2
• NCBI Official Synonym Symbols: PA28B; REGbeta; PA28beta
• NCBI Protein Information: proteasome activator complex subunit 2
• UniProt Protein Name: Proteasome activator complex subunit 2
• Protein Family: Proteasome activator complex
• UniProt Gene Name: PSME2
• UniProt Synonym Gene Names: REG-beta; PA28b; PA28beta
• UniProt Entry Name: PSME2_HUMAN

NCBI Description

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring. Six pseudogenes have been identified on chromosomes 4, 5, 8, 10 and 13. [provided by RefSeq, Jul 2008]

Uniprot Description

PSME2: Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome. Heterodimer of PSME1 and PSME2, which forms a hexadimeric ring. By IFNG/IFN-gamma. Belongs to the PA28 family.

Protein type: Protease; Proteasome complex

Chromosomal Location of Human Ortholog: 14q11.2

Cellular Component: cytoplasm; cytosol; membrane; nucleoplasm; proteasome activator complex; proteasome complex

Biological Process: activation of MAPKK activity; anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class I; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; antigen processing and presentation of peptide antigen via MHC class I; apoptosis; axon guidance; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; G1/S transition of mitotic cell cycle; gene expression; innate immune response; insulin receptor signaling pathway; MAPKKK cascade; mitotic cell cycle; negative regulation of apoptosis; negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle; nerve growth factor receptor signaling pathway; polyamine metabolic process; positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle; programmed cell death; protein polyubiquitination; Ras protein signal transduction; regulation of amino acid metabolic process; regulation of apoptosis; regulation of mRNA stability; regulation of ubiquitin-protein ligase activity during mitotic cell cycle; small GTPase mediated signal transduction; stimulatory C-type lectin receptor signaling pathway; T cell receptor signaling pathway; tumor necrosis factor-mediated signaling pathway; vascular endothelial growth factor receptor signaling pathway; viral reproduction