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Exosome complex component RRP42 (Exosome component 7) (Ribosomal RNA-processing protein 42) (p8)

 EXOS7_HUMAN             Reviewed;         291 AA.
Q15024; Q96E72;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
10-OCT-2018, entry version 177.
RecName: Full=Exosome complex component RRP42;
AltName: Full=Exosome component 7;
AltName: Full=Ribosomal RNA-processing protein 42;
AltName: Full=p8;
Name=EXOSC7; Synonyms=KIAA0116, RRP42;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
TISSUE=Brain;
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
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., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-274.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-291, AND VARIANT LEU-274.
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[4]
PROTEIN SEQUENCE OF 2-23, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RNA
EXOSOME CORE COMPLEX.
PubMed=11719186; DOI=10.1016/S0092-8674(01)00578-5;
Chen C.-Y., Gherzi R., Ong S.-E., Chan E.L., Raijmakers R.,
Pruijn G.J.M., Stoecklin G., Moroni C., Mann M., Karin M.;
"AU binding proteins recruit the exosome to degrade ARE-containing
mRNAs.";
Cell 107:451-464(2001).
[6]
PROTEIN INTERACTION.
PubMed=12419256; DOI=10.1016/S0022-2836(02)00947-6;
Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
"Protein-protein interactions between human exosome components support
the assembly of RNase PH-type subunits into a six-membered PNPase-like
ring.";
J. Mol. Biol. 323:653-663(2002).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH EXOSC1.
PubMed=11812149; DOI=10.1006/jmbi.2001.5265;
Raijmakers R., Noordman Y.E., van Venrooij W.J., Pruijn G.J.M.;
"Protein-protein interactions of hCsl4p with other human exosome
subunits.";
J. Mol. Biol. 315:809-818(2002).
[8]
PROTEIN INTERACTION.
PubMed=15231747; DOI=10.1101/gr.2122004;
Lehner B., Sanderson C.M.;
"A protein interaction framework for human mRNA degradation.";
Genome Res. 14:1315-1323(2004).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION IN THE RNA EXOSOME COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20531389; DOI=10.1038/emboj.2010.122;
Staals R.H., Bronkhorst A.W., Schilders G., Slomovic S., Schuster G.,
Heck A.J., Raijmakers R., Pruijn G.J.;
"Dis3-like 1: a novel exoribonuclease associated with the human
exosome.";
EMBO J. 29:2358-2367(2010).
[12]
INTERACTION WITH ZC3HAV1.
PubMed=21876179; DOI=10.1073/pnas.1101676108;
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L.,
Zheng Y.T., Gao G.;
"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
targeting multiply spliced viral mRNAs for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), LACK OF CATALYTIC ACTIVITY,
AND RECONSTITUTION OF THE RNA EXOSOME CORE COMPLEX.
PubMed=17174896; DOI=10.1016/j.cell.2006.10.037;
Liu Q., Greimann J.C., Lima C.D.;
"Reconstitution, activities, and structure of the eukaryotic RNA
exosome.";
Cell 127:1223-1237(2006).
[16]
ERRATUM.
Liu Q., Greimann J.C., Lima C.D.;
Cell 131:188-189(2007).
[17]
VARIANT [LARGE SCALE ANALYSIS] LEU-274, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Non-catalytic component of the RNA exosome complex which
has 3'->5' exoribonuclease activity and participates in a
multitude of cellular RNA processing and degradation events. In
the nucleus, the RNA exosome complex is involved in proper
maturation of stable RNA species such as rRNA, snRNA and snoRNA,
in the elimination of RNA processing by-products and non-coding
'pervasive' transcripts, such as antisense RNA species and
promoter-upstream transcripts (PROMPTs), and of mRNAs with
processing defects, thereby limiting or excluding their export to
the cytoplasm. The RNA exosome may be involved in Ig class switch
recombination (CSR) and/or Ig variable region somatic
hypermutation (SHM) by targeting AICDA deamination activity to
transcribed dsDNA substrates. In the cytoplasm, the RNA exosome
complex is involved in general mRNA turnover and specifically
degrades inherently unstable mRNAs containing AU-rich elements
(AREs) within their 3' untranslated regions, and in RNA
surveillance pathways, preventing translation of aberrant mRNAs.
It seems to be involved in degradation of histone mRNA. The
catalytic inactive RNA exosome core complex of 9 subunits (Exo-9)
is proposed to play a pivotal role in the binding and presentation
of RNA for ribonucleolysis, and to serve as a scaffold for the
association with catalytic subunits and accessory proteins or
complexes.
-!- SUBUNIT: Component of the RNA exosome complex. Specifically part
of the catalytically inactive RNA exosome core (Exo-9) complex
which is believed to associate with catalytic subunits EXOSC10,
and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome
complex forms. Exo-9 is formed by a hexameric ring of RNase PH
domain-containing subunits specifically containing the
heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and
peripheral S1 domain-containing components EXOSC1, EXOSC2 and
EXOSC3 located on the top of the ring structure. Interacts with
EXOSC1. Interacts with ZC3HAV1. {ECO:0000269|PubMed:11719186,
ECO:0000269|PubMed:11812149, ECO:0000269|PubMed:20531389,
ECO:0000269|PubMed:21876179}.
-!- INTERACTION:
Q9Y3B2:EXOSC1; NbExp=8; IntAct=EBI-371841, EBI-371892;
Q13868:EXOSC2; NbExp=6; IntAct=EBI-371841, EBI-301735;
Q9NPD3:EXOSC4; NbExp=4; IntAct=EBI-371841, EBI-371823;
Q92551:IP6K1; NbExp=3; IntAct=EBI-371841, EBI-751911;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:11812149}. Cytoplasm
{ECO:0000305|PubMed:11812149}. Nucleus
{ECO:0000305|PubMed:11812149}.
-!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000305}.
-!- CAUTION: The six exosome core subunits containing a RNase PH-
domain are not phosphorolytically active. {ECO:0000305}.
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EMBL; AC104165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012831; AAH12831.1; -; mRNA.
EMBL; D29958; BAA06226.1; -; mRNA.
CCDS; CCDS2725.1; -.
RefSeq; NP_055819.2; NM_015004.3.
UniGene; Hs.719958; -.
PDB; 2NN6; X-ray; 3.35 A; E=1-291.
PDB; 6D6Q; EM; 3.45 A; E=1-291.
PDB; 6D6R; EM; 3.45 A; E=1-291.
PDB; 6H25; EM; 3.80 A; E=1-291.
PDBsum; 2NN6; -.
PDBsum; 6D6Q; -.
PDBsum; 6D6R; -.
PDBsum; 6H25; -.
ProteinModelPortal; Q15024; -.
SMR; Q15024; -.
BioGrid; 116658; 43.
ComplexPortal; CPX-476; Nuclear exosome complex, DIS3-EXOSC10 variant.
ComplexPortal; CPX-591; Nucleolar exosome complex, EXOSC10 variant.
ComplexPortal; CPX-592; Cytoplasmic exosome complex, DIS3L variant.
ComplexPortal; CPX-593; Exosome complex, DIS3 variant.
ComplexPortal; CPX-600; Cytoplasmic exosome complex, DIS3L-EXOSC10 variant.
CORUM; Q15024; -.
DIP; DIP-31266N; -.
IntAct; Q15024; 30.
MINT; Q15024; -.
STRING; 9606.ENSP00000265564; -.
MoonDB; Q15024; Predicted.
iPTMnet; Q15024; -.
PhosphoSitePlus; Q15024; -.
BioMuta; EXOSC7; -.
DMDM; 322510129; -.
SWISS-2DPAGE; Q15024; -.
EPD; Q15024; -.
MaxQB; Q15024; -.
PaxDb; Q15024; -.
PeptideAtlas; Q15024; -.
PRIDE; Q15024; -.
ProteomicsDB; 60375; -.
DNASU; 23016; -.
Ensembl; ENST00000265564; ENSP00000265564; ENSG00000075914.
GeneID; 23016; -.
KEGG; hsa:23016; -.
UCSC; uc003coi.3; human.
CTD; 23016; -.
DisGeNET; 23016; -.
EuPathDB; HostDB:ENSG00000075914.12; -.
GeneCards; EXOSC7; -.
H-InvDB; HIX0003236; -.
HGNC; HGNC:28112; EXOSC7.
HPA; HPA036182; -.
HPA; HPA057980; -.
MIM; 606488; gene.
neXtProt; NX_Q15024; -.
OpenTargets; ENSG00000075914; -.
PharmGKB; PA134880567; -.
eggNOG; KOG1612; Eukaryota.
eggNOG; COG2123; LUCA.
GeneTree; ENSGT00530000063093; -.
HOGENOM; HOG000229504; -.
HOVERGEN; HBG051521; -.
InParanoid; Q15024; -.
KO; K12589; -.
OMA; NPYDCTR; -.
OrthoDB; EOG091G0CNN; -.
PhylomeDB; Q15024; -.
TreeFam; TF320641; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; EXOSC7; human.
EvolutionaryTrace; Q15024; -.
GenomeRNAi; 23016; -.
PRO; PR:Q15024; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000075914; Expressed in 234 organ(s), highest expression level in oocyte.
ExpressionAtlas; Q15024; baseline and differential.
Genevisible; Q15024; HS.
GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
GO; GO:0000176; C:nuclear exosome (RNase complex); IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; TAS:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; IBA:GO_Central.
GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0071028; P:nuclear mRNA surveillance; IBA:GO_Central.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IBA:GO_Central.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IBA:GO_Central.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IBA:GO_Central.
GO; GO:0034427; P:nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5'; IBA:GO_Central.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006401; P:RNA catabolic process; NAS:UniProtKB.
GO; GO:0006364; P:rRNA processing; TAS:UniProtKB.
GO; GO:0034473; P:U1 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IBA:GO_Central.
GO; GO:0034476; P:U5 snRNA 3'-end processing; IBA:GO_Central.
Gene3D; 3.30.230.70; -; 1.
InterPro; IPR001247; ExoRNase_PH_dom1.
InterPro; IPR015847; ExoRNase_PH_dom2.
InterPro; IPR036345; ExoRNase_PH_dom2_sf.
InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
Pfam; PF01138; RNase_PH; 1.
Pfam; PF03725; RNase_PH_C; 1.
SUPFAM; SSF54211; SSF54211; 2.
SUPFAM; SSF55666; SSF55666; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Exosome; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding; rRNA processing.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.4}.
CHAIN 2 291 Exosome complex component RRP42.
/FTId=PRO_0000139963.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.4}.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 169 169 R -> Q (in dbSNP:rs34512144).
/FTId=VAR_032765.
VARIANT 274 274 V -> L (in dbSNP:rs6794).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7788527}.
/FTId=VAR_014923.
HELIX 8 19 {ECO:0000244|PDB:2NN6}.
STRAND 24 26 {ECO:0000244|PDB:2NN6}.
STRAND 36 39 {ECO:0000244|PDB:2NN6}.
STRAND 45 53 {ECO:0000244|PDB:2NN6}.
STRAND 56 61 {ECO:0000244|PDB:2NN6}.
STRAND 71 73 {ECO:0000244|PDB:2NN6}.
STRAND 79 82 {ECO:0000244|PDB:2NN6}.
TURN 87 89 {ECO:0000244|PDB:2NN6}.
HELIX 99 115 {ECO:0000244|PDB:2NN6}.
STRAND 121 124 {ECO:0000244|PDB:2NN6}.
TURN 128 130 {ECO:0000244|PDB:2NN6}.
STRAND 135 141 {ECO:0000244|PDB:2NN6}.
HELIX 148 158 {ECO:0000244|PDB:2NN6}.
TURN 159 162 {ECO:0000244|PDB:2NN6}.
STRAND 167 171 {ECO:0000244|PDB:2NN6}.
STRAND 180 186 {ECO:0000244|PDB:2NN6}.
STRAND 201 213 {ECO:0000244|PDB:2NN6}.
HELIX 216 219 {ECO:0000244|PDB:2NN6}.
STRAND 223 228 {ECO:0000244|PDB:2NN6}.
STRAND 232 234 {ECO:0000244|PDB:2NN6}.
STRAND 238 245 {ECO:0000244|PDB:2NN6}.
HELIX 249 278 {ECO:0000244|PDB:2NN6}.
SEQUENCE 291 AA; 31821 MW; A674F745CEC61BBB CRC64;
MASVTLSEAE KVYIVHGVQE DLRVDGRGCE DYRCVEVETD VVSNTSGSAR VKLGHTDILV
GVKAEMGTPK LEKPNEGYLE FFVDCSASAT PEFEGRGGDD LGTEIANTLY RIFNNKSSVD
LKTLCISPRE HCWVLYVDVL LLECGGNLFD AISIAVKAAL FNTRIPRVRV LEDEEGSKDI
ELSDDPYDCI RLSVENVPCI VTLCKIGYRH VVDATLQEEA CSLASLLVSV TSKGVVTCMR
KVGKGSLDPE SIFEMMETGK RVGKVLHASL QSVVHKEESL GPKRQKVGFL G


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20-372-60232 exosome component 2 (EXOSC2). mRNA - Mouse monoclonal anti-human EXOSC2 antibody; EC 3.1.13.-; Ribosomal RNA-processing protein 4; Exosome component 2 Monoclonal 0.1 mg
20-372-60233 exosome component 7 (EXOSC7). mRNA - Mouse monoclonal anti-human EXOSC7 antibody; EC 3.1.13.-; Ribosomal RNA-processing protein 42; Exosome component 7; p8 Monoclonal 0.1 mg
CSB-EL007895HU Human Exosome complex component RRP42(EXOSC7) ELISA kit 96T
CSB-EL007895MO Mouse Exosome complex component RRP42(EXOSC7) ELISA kit 96T
EIAAB13504 Exosc9,Exosome complex component RRP45,Exosome component 9,Rat,Rattus norvegicus
EIAAB13501 Bos taurus,Bovine,EXOSC9,Exosome complex component RRP45,Exosome component 9


 

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