Phosphatase 1B Recombinant Protein | PPM1B recombinant protein

Recombinant Human Protein phosphatase 1B

Cat. Num. AAA1173136

• Gene Names: PPM1B; PP2CB; PP2CBETA; PP2C-beta; PPC2BETAX; PP2C-beta-X
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Phosphatase 1B; Recombinant Human Protein phosphatase 1B; Protein phosphatase 2; C isoform beta; PP2; C-beta; PPM1B recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-192aa; Full Length of Isoform Beta-X
• Sequence: SIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYSRLNPHRESDGASDEAEESGSQGKLVEALRQMRINHRGNYRQLLEEMLTSYRLAKVEGEESPAEPAATATSSNSDAGNPVTMQESHTESESGLAELDSSNEDAGTKMSGEKI
• Sequence Length: 380

• 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 PPM1B recombinant protein

Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.

Product Categories/Family for PPM1B recombinant protein

Signal Transduction

References

The cloning expression and tissue distribution of human PP2Cbeta.Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K.FEBS Lett. 431:121-124(1998) Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms.Cheng A., Kaldis P., Solomon M.J.J. Biol. Chem. 275:34744-34749(2000) Protein phosphatase 1B. Cloning and characterization of two major transcripts generated by alternative use of 3' exons.Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I., Smorodinsky N.I., Lavi S.The 2p21 deletion syndrome characterization of the transcription content.Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K., Hershkovitz E.Genomics 86:195-211(2005) Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005)

NCBI and Uniprot Product Information

• NCBI GI #: 75813620
• NCBI GeneID: 5495
• NCBI Accession #: NP_001028729.1
• NCBI GenBank Nucleotide #: NM_001033557.2
• UniProt Accession #: O75688; Q461Q2; Q4J6C1; Q4J6C2; Q658R4; Q96ER6; Q9HAY8
• Molecular Weight: 36.6 kDa
• NCBI Official Full Name: protein phosphatase 1B isoform 5
• NCBI Official Synonym Full Names: protein phosphatase, Mg2+/Mn2+ dependent 1B
• NCBI Official Symbol: PPM1B
• NCBI Official Synonym Symbols: PP2CB; PP2CBETA; PP2C-beta; PPC2BETAX; PP2C-beta-X
• NCBI Protein Information: protein phosphatase 1B
• UniProt Protein Name: Protein phosphatase 1B
• Protein Family: Protein phosphatase
• UniProt Gene Name: PPM1B
• UniProt Synonym Gene Names: PP2CB; PP2C-beta
• UniProt Entry Name: PPM1B_HUMAN

NCBI Description

The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase has been shown to dephosphorylate cyclin-dependent kinases (CDKs), and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to cause cell-growth arrest or cell death. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional transcript variants have been described, but currently do not represent full-length sequences. [provided by RefSeq, Jul 2008]

Uniprot Description

PPM1B: ubiquitous cytosolic Ser/Thr protein phosphatase, catalytic subunit. The holoenzyme consists of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B'/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules.

Protein type: Motility/polarity/chemotaxis; EC 3.1.3.16; Protein phosphatase, Ser/Thr (non-receptor)

Chromosomal Location of Human Ortholog: 2p21

Cellular Component: cytosol; membrane

Molecular Function: magnesium ion binding; manganese ion binding; protein binding; protein serine/threonine phosphatase activity

Biological Process: cytokine and chemokine mediated signaling pathway; N-terminal protein myristoylation; negative regulation of defense response to virus; negative regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of interferon-beta production; negative regulation of NF-kappaB import into nucleus; protein amino acid dephosphorylation