60S acidic ribosomal protein P1 Recombinant Protein | RPLP1 recombinant protein

Recombinant Human 60S acidic ribosomal protein P1

Cat. Num. AAA717082

• Gene Names: RPLP1; P1; LP1; RPP1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: 60S acidic ribosomal protein P1; Recombinant Human 60S acidic ribosomal protein P1; RPLP1 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: 2-114
• Sequence: ASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD
• Sequence Length: 114

• 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 RPLP1 recombinant protein

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

Product Categories/Family for RPLP1 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) 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) Analysis of the DNA sequence and duplication history of human chromosome 15.Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.Nature 440:671-675(2006) 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. Identification and characterization of phosphorylated proteins in the human pituitary.Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.Proteomics 4:587-598(2004) Phosphoproteomic analysis of the human pituitary.Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.Pituitary 9:109-120(2006) 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) 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) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex.Lee K.M., Yu C.W., Chiu T.Y., Sze K.H., Shaw P.C., Wong K.B.Nucleic Acids Res. 40:3172-3182(2012) Structures of the human and Drosophila 80S ribosome.Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.Nature 497:80-85(2013)

NCBI and Uniprot Product Information

• NCBI GI #: 4506669
• NCBI GeneID: 6176
• NCBI Accession #: NP_000994.1
• NCBI GenBank Nucleotide #: NM_001003.2
• UniProt Accession #: P05386; A6NIB2
• Molecular Weight: 38.8kD
• NCBI Official Full Name: 60S acidic ribosomal protein P1 isoform 1
• NCBI Official Synonym Full Names: ribosomal protein, large, P1
• NCBI Official Symbol: RPLP1
• NCBI Official Synonym Symbols: P1; LP1; RPP1
• NCBI Protein Information: 60S acidic ribosomal protein P1
• UniProt Protein Name: 60S acidic ribosomal protein P1
• Protein Family: 60S acidic ribosomal protein
• UniProt Gene Name: RPLP1
• UniProt Synonym Gene Names: RRP1
• UniProt Entry Name: RLA1_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 P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. 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

RPLP1: Plays an important role in the elongation step of protein synthesis. Belongs to the ribosomal protein L12P family.

Protein type: Translation; Ribosomal

Chromosomal Location of Human Ortholog: 15q22

Cellular Component: cytoplasm; cytosol; focal adhesion

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