60S ribosomal protein L11 Recombinant Protein | RPL11 recombinant protein

Recombinant Human 60S ribosomal protein L11

Cat. Num. AAA717080

• Gene Names: RPL11; L11; DBA7; GIG34
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: 60S ribosomal protein L11; Recombinant Human 60S ribosomal protein L11; CLL-associated antigen KW-12; RPL11 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: 3-178aa; Partial
• Sequence: QDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRRTGCIGAKHRISKEEAMRWFQQKYDGIILPGK
• Sequence Length: 178

• 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 RPL11 recombinant protein

Binds to 5S ribosomal RNA. Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML.

Product Categories/Family for RPL11 recombinant protein

Cell Cycle

References

Cloning and determination of the primary structure of DNA complementary to the mRNA of human ribosomal protein L11.Mishin V.P., Filipenko M.L., Muravlev A.I., Karpova G.G., Mertvetsov N.P.Bioorg. Khim. 21:158-160(1995) Expressed sequence tags from a human cell line.Bhat K.S.Structural and functional analysis of the human ribosomal protein L11 gene.Voronina E.N., Kolokol'tsova T.D., Nechaeva E.A., Filipenko M.L.Mol. Biol. (Mosk.) 37:425-435(2003) Quadroni M., Bienvenut W.V.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) Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing.Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.J. Protein Chem. 22:249-258(2003) Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients.Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., Meerpohl J.J., Atsidaftos E., Lipton J.M., Gleizes P.-E., Beggs A.H.Am. J. Hum. Genet. 83:769-780(2008) 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) 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) 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) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) 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) Identification of mutations in the ribosomal protein L5 (RPL5) and ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan anemia.Cmejla R., Cmejlova J., Handrkova H., Petrak J., Petrtylova K., Mihal V., Stary J., Cerna Z., Jabali Y., Pospisilova D.Hum. Mutat. 30:321-327(2009)

NCBI and Uniprot Product Information

• NCBI GI #: 15431290
• NCBI GeneID: 6135
• NCBI Accession #: NP_000966.2
• NCBI GenBank Nucleotide #: NM_000975.3
• UniProt Accession #: P62913; P25121; P39026; Q8TDH2; Q9Y674
• Molecular Weight: 47.1 kDa
• NCBI Official Full Name: 60S ribosomal protein L11 isoform 1
• NCBI Official Synonym Full Names: ribosomal protein L11
• NCBI Official Symbol: RPL11
• NCBI Official Synonym Symbols: L11; DBA7; GIG34
• NCBI Protein Information: 60S ribosomal protein L11
• UniProt Protein Name: 60S ribosomal protein L11
• Protein Family: 60S ribosomal protein
• UniProt Gene Name: RPL11
• UniProt Entry Name: RL11_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 protein that is a component of the 60S subunit. The protein belongs to the L5P family of ribosomal proteins. It is located in the cytoplasm. The protein probably associates with the 5S rRNA. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. [provided by RefSeq, Dec 2010]

Uniprot Description

RPL11: Binds to 5S ribosomal RNA. Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML. Defects in RPL11 are the cause of Diamond-Blackfan anemia type 7 (DBA7). DBA7 is a form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of malignancy. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies. Belongs to the ribosomal protein L5P family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Translation; Motility/polarity/chemotaxis; Nucleolus; Ribosomal

Chromosomal Location of Human Ortholog: 1p36.1-p35

Cellular Component: cytoplasm; cytosol; membrane; nucleolus

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

Biological Process: cellular protein metabolic process; gene expression; mRNA catabolic process, nonsense-mediated decay; protein targeting; ribosomal large subunit assembly and maintenance; ribosomal large subunit biogenesis and assembly; rRNA processing; 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

Disease: Diamond-blackfan Anemia 7