Retinoblastoma-associated protein Recombinant Protein | Rb1 recombinant protein

Recombinant Rat Retinoblastoma-associated protein

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Retinoblastoma-associated protein; Recombinant Rat Retinoblastoma-associated protein; pRb; Rbpp105; Rb1 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: 721-919
• Sequence: KDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYMSPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGSDEADGSKHLPAESKFQQKLAEMTSTRTRMQKQKLNDSMEISNKEE
• Sequence Length: 920

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

Related Product Information for Rb1 recombinant protein

Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex.

References

Genome sequence of the Brown Norway rat yields insights into mammalian evolution.Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.Nature 428:493-521(2004) Isolation and sequence polymorphism of a rat retinoblastoma (RB) cDNA.Esumi M., Idutsu T., Kinugasa S., Ohno M., Nakabayashi H., Ikeda T., Shikata T.Gene 161:231-235(1995) Cloning and sequence of the rat retinoblastoma (Rb) gene cDNA.Roy N.K., Ballesteros A., Garte S.J.Nucleic Acids Res. 21:170-170(1993) Cdc2 and Cdk2 kinase activated by transforming growth factor-beta1 trigger apoptosis through the phosphorylation of retinoblastoma protein in FaO hepatoma cells.Choi K.S., Eom Y.W., Kang Y., Ha M.J., Rhee H., Yoon J.-W., Kim S.-J.J. Biol. Chem. 274:31775-31783(1999) DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters.Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P.Nat. Genet. 25:338-342(2000) A calcium-dependent switch in a CREST-BRG1 complex regulates activity-dependent gene expression.Qiu Z., Ghosh A.Neuron 60:775-787(2008)

NCBI and Uniprot Product Information

• NCBI GI #: 281332095
• NCBI GeneID: 24708
• NCBI Accession #: NP_058741.1
• NCBI GenBank Nucleotide #: NM_017045.1
• UniProt Accession #: P33568; Q63527
• Molecular Weight: 26.7kD
• NCBI Official Full Name: retinoblastoma-associated protein
• NCBI Official Synonym Full Names: retinoblastoma 1
• NCBI Official Symbol: Rb1
• NCBI Protein Information: retinoblastoma-associated protein
• UniProt Protein Name: Retinoblastoma-associated protein
• Protein Family: Retinoblastoma-associated protein
• UniProt Gene Name: Rb1
• UniProt Synonym Gene Names: Rb-1; Rb
• UniProt Entry Name: RB_RAT

NCBI Description

plays a role in negative regulation of the cell cycle and of DNA replication; acts as a tumor suppressor [RGD, Feb 2006]

Uniprot Description

Rb: retinoblastoma tumor suppressor protein regulates cell proliferation by controlling progression through the G1-phase restriction point. Has three distinct binding domains and interacts with regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase and proteins with a conserved LXCXE motif. Cell cycle-dependent phosphorylation by Cdks inhibits Rb target binding, thus allowing cell cycle progression. Recruits and targets histone methyltransferase suv39h1 leading to epigenetic transcriptional repression.

Protein type: Transcription, coactivator/corepressor; Oncoprotein; Nuclear receptor co-regulator; Tumor suppressor

Cellular Component: nucleus; PML body; Rb-E2F complex; spindle; transcription factor complex

Molecular Function: DNA binding; enzyme binding; identical protein binding; kinase binding; phosphoprotein binding; protein binding; transcription factor binding; ubiquitin protein ligase binding

Biological Process: cell cycle arrest; cell division; chromatin modification; enucleate erythrocyte differentiation; G1/S transition of mitotic cell cycle; gut development; maintenance of mitotic sister chromatid cohesion; myoblast differentiation; negative regulation of cell cycle; negative regulation of cell proliferation; negative regulation of epithelial cell proliferation; negative regulation of mitotic cell cycle; negative regulation of protein kinase activity; negative regulation of smoothened signaling pathway; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; neurite development; neuron apoptosis; neuron differentiation; neuron maturation; neuron morphogenesis during differentiation; positive regulation of macrophage differentiation; positive regulation of mitotic metaphase/anaphase transition; positive regulation of transcription from RNA polymerase II promoter; Ras protein signal transduction; regulation of cell cycle; regulation of lipid kinase activity; regulation of mitotic cell cycle; regulation of transcription from RNA polymerase II promoter; sister chromatid biorientation; spermatogenesis; striated muscle cell differentiation; transcription, DNA-dependent