protein

Recombinant Human 60S acidic ribosomal protein P0

MBS949478

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human 60S acidic ribosomal protein P0

60S acidic ribosomal protein P0

60S ribosomal protein L10E

60S acidic ribosomal protein P0; 60S acidic ribosomal protein P0; 60S acidic ribosomal protein P0; ribosomal protein, large, P0; 60S ribosomal protein L10E

RPLP0

RPLP0; RPLP0; P0; LP0; L10E; RPP0; PRLP0

RLA0_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-317

317

MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQ
MQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKL
LPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIA
PCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILS
DVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDN
GSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTV
ASVPHSIINGYERVLALSVET

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Epigenetics and Nuclear Signaling

Ribosomal protein P0 is the functional equivalent of E Coli protein L10.

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 finished DNA sequence of human chromosome 12.Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.Nature 440:346-351(2006) Lubec G., Chen W.-Q., Sun Y.Submitted (DEC-2008) to UniProtKB A map of 75 human ribosomal protein genes.Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.Genome Res. 8:509-523(1998) Molecular composition of IMP1 ribonucleoprotein granules.Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.Mol. Cell. Proteomics 6:798-811(2007) APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process.Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.Mol. Cell. Biol. 29:1834-1854(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 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) 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)

4506667

NP_000993.1

NM_001002.3

P05388

50.3kD

Cap-dependent Translation Initiation Pathway (1268680); Cytoplasmic Ribosomal Proteins Pathway (198853); Disease Pathway (1268854); Eukaryotic Translation Elongation Pathway (1268690); Eukaryotic Translation Initiation Pathway (1268679); Eukaryotic Translation Termination Pathway (1268692); Formation Of A Pool Of Free 40S Subunits Pathway (1268681); GTP Hydrolysis And Joining Of The 60S Ribosomal Subunit Pathway (1268686); Gene Expression Pathway (1269649); Infectious Disease Pathway (1269056)

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 protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. 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]

RPLP0: a ribosomal protein of the L10P family. Located in the cytoplasm and nucleus. 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 protein is a component of the 60S subunit. Protein type: Ribosomal; Translation. Chromosomal Location of Human Ortholog: 12q24.2. Cellular Component: cytoplasm; cytosol; focal adhesion; membrane; nucleus; ribonucleoprotein complex. Molecular Function: protein binding; RNA binding; structural constituent of ribosome. Biological Process: cellular protein metabolic process; gene expression; mRNA catabolic process, nonsense-mediated decay; ribosome biogenesis and assembly; 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

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750