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60S acidic ribosomal protein P0 (A0) (L10e) (Large ribosomal subunit protein uL10)

 RLA0_YEAST              Reviewed;         312 AA.
P05317; D6VYX8;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
25-OCT-2017, entry version 173.
RecName: Full=60S acidic ribosomal protein P0 {ECO:0000303|PubMed:9559554};
Short=A0;
AltName: Full=L10e;
AltName: Full=Large ribosomal subunit protein uL10 {ECO:0000303|PubMed:24524803};
Name=RPP0 {ECO:0000303|PubMed:9559554};
Synonyms=L10E, RPA0, RPL10E, RPLA0; OrderedLocusNames=YLR340W;
ORFNames=L8300.8;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=IFO 40028;
PubMed=3287327; DOI=10.1093/nar/16.8.3573;
Mitsui K., Tsurugi K.;
"cDNA and deduced amino acid sequence of 38 kDa-type acidic ribosomal
protein A0 from Saccharomyces cerevisiae.";
Nucleic Acids Res. 16:3573-3573(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2681177; DOI=10.1093/oxfordjournals.jbchem.a122836;
Mitsui K., Nakagawa T., Tsurugi K.;
"The gene and the primary structure of acidic ribosomal protein A0
from yeast Saccharomyces cerevisiae which shows partial homology to
bacterial ribosomal protein L10.";
J. Biochem. 106:223-227(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SR26-12C;
PubMed=2404943;
Newton C.H., Shimmin L.C., Yee J., Dennis P.P.;
"A family of genes encode the multiple forms of the Saccharomyces
cerevisiae ribosomal proteins equivalent to the Escherichia coli L12
protein and a single form of the L10-equivalent ribosomal protein.";
J. Bacteriol. 172:579-588(1990).
[4]
ERRATUM.
PubMed=2188966; DOI=10.1128/jb.172.6.3535.1990;
Newton C.H., Shimmin L.C., Yee J., Dennis P.P.;
J. Bacteriol. 172:3535-3535(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
NOMENCLATURE, AND SUBUNIT.
PubMed=9559554;
DOI=10.1002/(SICI)1097-0061(19980330)14:5<471::AID-YEA241>3.0.CO;2-U;
Planta R.J., Mager W.H.;
"The list of cytoplasmic ribosomal proteins of Saccharomyces
cerevisiae.";
Yeast 14:471-477(1998).
[8]
PHOSPHORYLATION AT SER-302.
PubMed=9843429; DOI=10.1021/bi981396i;
Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G.;
"Phosphorylation of ribosomal protein P0 is not essential for ribosome
function but can affect translation.";
Biochemistry 37:16620-16626(1998).
[9]
INTERACTION WITH YFL034W.
PubMed=15286401; DOI=10.1007/BF02702559;
Aruna K., Chakraborty T., Nambeesan S., Mannan A.B., Sehgal A.,
Balachandara S.R., Sharma S.;
"Identification of a hypothetical membrane protein interactor of
ribosomal phosphoprotein P0.";
J. Biosci. 29:33-43(2004).
[10]
INTERACTION WITH RPP1A; RPP1B; RPP2A AND RPP2B.
PubMed=16573688; DOI=10.1111/j.1365-2958.2006.05117.x;
Krokowski D., Boguszewska A., Abramczyk D., Liljas A., Tchorzewski M.,
Grankowski N.;
"Yeast ribosomal P0 protein has two separate binding sites for P1/P2
proteins.";
Mol. Microbiol. 60:386-400(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-302, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[14]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-97 AND LYS-144,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[15]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[16]
X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS).
PubMed=21109664; DOI=10.1126/science.1194294;
Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
"Crystal structure of the eukaryotic ribosome.";
Science 330:1203-1209(2010).
[17]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=22096102; DOI=10.1126/science.1212642;
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L.,
Yusupova G., Yusupov M.;
"The structure of the eukaryotic ribosome at 3.0 A resolution.";
Science 334:1524-1529(2011).
-!- FUNCTION: Component of the ribosome, a large ribonucleoprotein
complex responsible for the synthesis of proteins in the cell. The
small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and
translates the encoded message by selecting cognate aminoacyl-
transfer RNA (tRNA) molecules. The large subunit (LSU) contains
the ribosomal catalytic site termed the peptidyl transferase
center (PTC), which catalyzes the formation of peptide bonds,
thereby polymerizing the amino acids delivered by tRNAs into a
polypeptide chain. The nascent polypeptides leave the ribosome
through a tunnel in the LSU and interact with protein factors that
function in enzymatic processing, targeting, and the membrane
insertion of nascent chains at the exit of the ribosomal tunnel.
uL10 forms part of the P stalk that participates in recruiting G
proteins to the ribosome. {ECO:0000305|PubMed:22096102}.
-!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature
yeast ribosomes consist of a small (40S) and a large (60S)
subunit. The 40S small subunit contains 1 molecule of ribosomal
RNA (18S rRNA) and 33 different proteins (encoded by 57 genes).
The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S
rRNA) and 46 different proteins (encoded by 81 genes)
(PubMed:9559554, PubMed:22096102). The 5 acidic ribosomal P-
proteins form the stalk structure of the 60S subunit. They are
organized as a pentameric complex in which uL10/P0 interacts with
2 heterodimers, P1A-P2B and P1B-P2A. uL10 directly interacts with
28S rRNA (PubMed:16573688). uL10 interacts with YFL034W
(PubMed:15286401). {ECO:0000269|PubMed:15286401,
ECO:0000269|PubMed:16573688, ECO:0000269|PubMed:22096102,
ECO:0000305|PubMed:9559554}.
-!- INTERACTION:
P32324:EFT2; NbExp=2; IntAct=EBI-15447, EBI-6333;
P05318:RPP1A; NbExp=3; IntAct=EBI-15447, EBI-15452;
P10622:RPP1B; NbExp=2; IntAct=EBI-15447, EBI-15460;
P05319:RPP2A; NbExp=2; IntAct=EBI-15447, EBI-15456;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
-!- SIMILARITY: Belongs to the universal ribosomal protein uL10
family. {ECO:0000305}.
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EMBL; X06959; CAA30029.1; -; mRNA.
EMBL; D00529; BAA00415.1; -; Genomic_DNA.
EMBL; X13328; CAA31703.1; -; Genomic_DNA.
EMBL; M26506; AAA34730.1; -; Genomic_DNA.
EMBL; M37326; AAA34729.1; -; Genomic_DNA.
EMBL; U19028; AAB67258.1; -; Genomic_DNA.
EMBL; BK006945; DAA09644.1; -; Genomic_DNA.
PIR; S51343; R5BY0E.
RefSeq; NP_013444.1; NM_001182229.1.
PDB; 3J16; EM; -; G=1-312.
PDB; 3J77; EM; 6.20 A; P0=1-312.
PDB; 3J78; EM; 6.30 A; P0=1-312.
PDB; 4U3M; X-ray; 3.00 A; p0=2-311.
PDB; 4U3N; X-ray; 3.20 A; p0=2-312.
PDB; 4U3U; X-ray; 2.90 A; p0=2-312.
PDB; 4U4N; X-ray; 3.10 A; p0=2-312.
PDB; 4U4O; X-ray; 3.60 A; p0=2-312.
PDB; 4U4Q; X-ray; 3.00 A; p0=2-312.
PDB; 4U4R; X-ray; 2.80 A; p0=2-312.
PDB; 4U4U; X-ray; 3.00 A; p0=2-312.
PDB; 4U4Y; X-ray; 3.20 A; p0=2-312.
PDB; 4U4Z; X-ray; 3.10 A; p0=2-312.
PDB; 4U50; X-ray; 3.20 A; p0=2-312.
PDB; 4U51; X-ray; 3.20 A; p0=2-312.
PDB; 4U52; X-ray; 3.00 A; p0=2-312.
PDB; 4U53; X-ray; 3.30 A; p0=2-312.
PDB; 4U55; X-ray; 3.20 A; p0=2-312.
PDB; 4U56; X-ray; 3.45 A; p0=2-312.
PDB; 4U6F; X-ray; 3.10 A; p0=2-312.
PDB; 4V6I; EM; 8.80 A; Bs=1-312.
PDB; 4V7R; X-ray; 4.00 A; DM=1-312.
PDB; 4V88; X-ray; 3.00 A; Dq=1-312.
PDB; 4V8T; EM; 8.10 A; q=1-312.
PDB; 4V8Y; EM; 4.30 A; Bq=1-312.
PDB; 4V8Z; EM; 6.60 A; Bq=1-237.
PDB; 5APN; EM; 3.91 A; q=1-312.
PDB; 5APO; EM; 3.41 A; q=1-312.
PDB; 5DAT; X-ray; 3.15 A; p0=2-221.
PDB; 5DC3; X-ray; 3.25 A; p0=2-312.
PDB; 5DGE; X-ray; 3.45 A; p0=2-312.
PDB; 5DGV; X-ray; 3.10 A; p0=2-312.
PDB; 5FCI; X-ray; 3.40 A; p0=2-311.
PDB; 5FCJ; X-ray; 3.10 A; p0=2-312.
PDB; 5I4L; X-ray; 3.10 A; p0=1-312.
PDB; 5JUO; EM; 4.00 A; VA=1-312.
PDB; 5JUP; EM; 3.50 A; VA=1-312.
PDB; 5JUS; EM; 4.20 A; VA=1-312.
PDB; 5JUT; EM; 4.00 A; VA=1-312.
PDB; 5JUU; EM; 4.00 A; VA=1-312.
PDB; 5LYB; X-ray; 3.25 A; p0=3-198.
PDB; 5MEI; X-ray; 3.50 A; p0=2-221.
PDB; 5TBW; X-ray; 3.00 A; p0=3-221.
PDB; 5TGA; X-ray; 3.30 A; p0=3-221.
PDBsum; 3J16; -.
PDBsum; 3J77; -.
PDBsum; 3J78; -.
PDBsum; 4U3M; -.
PDBsum; 4U3N; -.
PDBsum; 4U3U; -.
PDBsum; 4U4N; -.
PDBsum; 4U4O; -.
PDBsum; 4U4Q; -.
PDBsum; 4U4R; -.
PDBsum; 4U4U; -.
PDBsum; 4U4Y; -.
PDBsum; 4U4Z; -.
PDBsum; 4U50; -.
PDBsum; 4U51; -.
PDBsum; 4U52; -.
PDBsum; 4U53; -.
PDBsum; 4U55; -.
PDBsum; 4U56; -.
PDBsum; 4U6F; -.
PDBsum; 4V6I; -.
PDBsum; 4V7R; -.
PDBsum; 4V88; -.
PDBsum; 4V8T; -.
PDBsum; 4V8Y; -.
PDBsum; 4V8Z; -.
PDBsum; 5APN; -.
PDBsum; 5APO; -.
PDBsum; 5DAT; -.
PDBsum; 5DC3; -.
PDBsum; 5DGE; -.
PDBsum; 5DGV; -.
PDBsum; 5FCI; -.
PDBsum; 5FCJ; -.
PDBsum; 5I4L; -.
PDBsum; 5JUO; -.
PDBsum; 5JUP; -.
PDBsum; 5JUS; -.
PDBsum; 5JUT; -.
PDBsum; 5JUU; -.
PDBsum; 5LYB; -.
PDBsum; 5MEI; -.
PDBsum; 5TBW; -.
PDBsum; 5TGA; -.
ProteinModelPortal; P05317; -.
SMR; P05317; -.
BioGrid; 31602; 322.
DIP; DIP-1582N; -.
IntAct; P05317; 286.
MINT; MINT-384116; -.
STRING; 4932.YLR340W; -.
iPTMnet; P05317; -.
SWISS-2DPAGE; P05317; -.
MaxQB; P05317; -.
PRIDE; P05317; -.
TopDownProteomics; P05317; -.
EnsemblFungi; YLR340W; YLR340W; YLR340W.
GeneID; 851052; -.
KEGG; sce:YLR340W; -.
EuPathDB; FungiDB:YLR340W; -.
SGD; S000004332; RPP0.
GeneTree; ENSGT00390000017839; -.
HOGENOM; HOG000210987; -.
InParanoid; P05317; -.
KO; K02941; -.
OMA; FFQALQI; -.
OrthoDB; EOG092C4JUE; -.
BioCyc; YEAST:G3O-32417-MONOMER; -.
Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:P05317; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:SGD.
GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
InterPro; IPR030670; L10E_eukaryotes.
InterPro; IPR001790; Ribosomal_L10P.
Pfam; PF00466; Ribosomal_L10; 1.
PIRSF; PIRSF039087; L10E; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Isopeptide bond;
Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
CHAIN 1 312 60S acidic ribosomal protein P0.
/FTId=PRO_0000154786.
REGION 199 230 Interaction with P1A-P2B.
REGION 231 258 Interaction with P1B-P2A.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 302 302 Phosphoserine; by CK2.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:9843429}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 97 97 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 83 83 N -> Y (in Ref. 1; CAA30029 and 2;
BAA00415/CAA31703). {ECO:0000305}.
HELIX 4 21 {ECO:0000244|PDB:4U4R}.
STRAND 23 29 {ECO:0000244|PDB:4U4R}.
HELIX 35 43 {ECO:0000244|PDB:4U4R}.
STRAND 46 48 {ECO:0000244|PDB:4U3U}.
STRAND 50 53 {ECO:0000244|PDB:4U4R}.
HELIX 56 64 {ECO:0000244|PDB:4U4R}.
STRAND 68 70 {ECO:0000244|PDB:4U4R}.
HELIX 72 74 {ECO:0000244|PDB:4U4R}.
HELIX 77 79 {ECO:0000244|PDB:4U4R}.
STRAND 82 89 {ECO:0000244|PDB:4U4R}.
HELIX 93 102 {ECO:0000244|PDB:4U4R}.
STRAND 186 194 {ECO:0000244|PDB:4U4R}.
STRAND 195 197 {ECO:0000244|PDB:4U3M}.
TURN 200 202 {ECO:0000244|PDB:4U4R}.
HELIX 210 213 {ECO:0000244|PDB:4U4R}.
TURN 214 219 {ECO:0000244|PDB:4U4R}.
SEQUENCE 312 AA; 33717 MW; 109ECC90F7C8B68E CRC64;
MGGIREKKAE YFAKLREYLE EYKSLFVVGV DNVSSQQMHE VRKELRGRAV VLMGKNTMVR
RAIRGFLSDL PDFEKLLPFV KGNVGFVFTN EPLTEIKNVI VSNRVAAPAR AGAVAPEDIW
VRAVNTGMEP GKTSFFQALG VPTKIARGTI EIVSDVKVVD AGNKVGQSEA SLLNLLNISP
FTFGLTVVQV YDNGQVFPSS ILDITDEELV SHFVSAVSTI ASISLAIGYP TLPSVGHTLI
NNYKDLLAVA IAASYHYPEI EDLVDRIENP EKYAAAAPAA TSAASGDAAP AEEAAAEEEE
ESDDDMGFGL FD


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EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
29-221 RPL32 is a ribosomal protein that is a component of the 60S subunit. RPL32 belongs to the L32E family of ribosomal proteins. It is located in the cytoplasm. Although some studies have mapped this gene 0.1 mg
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
EIAAB35181 C15orf15,Homo sapiens,Human,My024,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,RPL24L,RSL24D1
EIAAB36079 40S ribosomal protein S2,40S ribosomal protein S4,Homo sapiens,Human,Protein LLRep3,RPS2,RPS4
18-783-75538 RABBIT ANTI RIBOSOMAL S6 KINASE 2 (C-TERMINAL) - RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; EC 2.7.11.1; S6K-alpha 2; 90 kDa ribosomal protein S6 kinase 2; p90-RSK 2; Ribosomal S6 kinase 3; RSK-3; pp90RSK3; 0.1 ml
15-5083 Antigens 60S acidic ribosomal protein P1 protein, Human, Recombinant, E.coli 20


 

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