60S acidic ribosomal protein P2 Recombinant Protein | RPLP2 recombinant protein

Recombinant Human 60S acidic ribosomal protein P2

Cat. Num. AAA1265420

• Gene Names: RPLP2; P2; LP2; RPP2; D11S2243E
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: 60S acidic ribosomal protein P2; Recombinant Human 60S acidic ribosomal protein P2; Renal carcinoma antigen NY-REN-44; RPLP2 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: 1-113aa; Partial
• Sequence: MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGL
• Sequence Length: 115

• 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 RPLP2 recombinant protein

Plays an important role in the elongation step of protein synthesis.

Product Categories/Family for RPLP2 recombinant protein

Epigenetics and Nuclear Signaling

References

Human acidic ribosomal phosphoproteins P0, P1, and P2 analysis of cDNA clones, in vitro synthesis, and assembly.Rich B.E., Steitz J.A.Mol. Cell. Biol. 7:4065-4074(1987) A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2.Sharp M.G.F., Adams S.M., Elvin P., Walker R.A., Brammar W.J., Varley J.M.Br. J. Cancer 61:83-88(1990) The human ribosomal protein genes sequencing and comparative analysis of 73 genes.Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.Genome Res. 12:379-390(2002) 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) 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. Human liver protein map a reference database established by microsequencing and gel comparison.Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.Electrophoresis 13:992-1001(1992) Antigens recognized by autologous antibody in patients with renal-cell carcinoma.Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.3.0.CO;2-5>Int. J. Cancer 83:456-464(1999) Identification and characterization of phosphorylated proteins in the human pituitary.Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.Proteomics 4:587-598(2004) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.Nat. Biotechnol. 24:1285-1292(2006) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) 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) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. 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NCBI and Uniprot Product Information

• NCBI GI #: 4506671
• NCBI GeneID: 6181
• NCBI Accession #: NP_000995.1
• NCBI GenBank Nucleotide #: NM_001004.3
• UniProt Accession #: P05387; Q6FG96
• Molecular Weight: 38.4 kDa
• NCBI Official Full Name: 60S acidic ribosomal protein P2
• NCBI Official Synonym Full Names: ribosomal protein lateral stalk subunit P2
• NCBI Official Symbol: RPLP2
• NCBI Official Synonym Symbols: P2; LP2; RPP2; D11S2243E
• NCBI Protein Information: 60S acidic ribosomal protein P2
• UniProt Protein Name: 60S acidic ribosomal protein P2
• Protein Family: 60S acidic ribosomal protein
• UniProt Gene Name: RPLP2
• UniProt Synonym Gene Names: D11S2243E; RPP2
• UniProt Entry Name: RLA2_HUMAN

NCBI Description

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P1. The P2 protein can interact with P0 and P1 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Jul 2008]

Uniprot Description

RPLP2: Plays an important role in the elongation step of protein synthesis. Belongs to the ribosomal protein L12P family.

Protein type: Ribosomal; Translation

Chromosomal Location of Human Ortholog: 11p15.5

Cellular Component: cytosol; focal adhesion; membrane

Molecular Function: protein binding; RNA binding; structural constituent of ribosome

Biological Process: cellular protein metabolic process; gene expression; mRNA catabolic process, nonsense-mediated decay; selenium metabolic process; selenocysteine metabolic process; SRP-dependent cotranslational protein targeting to membrane; translation; translational elongation; translational initiation; translational termination; viral infectious cycle; viral reproduction; viral transcription