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Protein argonaute-2 (Argonaute2) (mAgo2) (EC 3.1.26.n2) (Argonaute RISC catalytic component 2) (Eukaryotic translation initiation factor 2C 2) (eIF-2C 2) (eIF2C 2) (Piwi/argonaute family protein meIF2C2) (Protein slicer)

 AGO2_MOUSE              Reviewed;         860 AA.
Q8CJG0; A1A563; Q4VAB3; Q571J6;
14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 135.
RecName: Full=Protein argonaute-2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=Argonaute2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=mAgo2;
EC=3.1.26.n2 {ECO:0000255|HAMAP-Rule:MF_03031};
AltName: Full=Argonaute RISC catalytic component 2;
AltName: Full=Eukaryotic translation initiation factor 2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=eIF-2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
Short=eIF2C 2 {ECO:0000255|HAMAP-Rule:MF_03031};
AltName: Full=Piwi/argonaute family protein meIF2C2;
AltName: Full=Protein slicer {ECO:0000255|HAMAP-Rule:MF_03031};
Name=Ago2; Synonyms=Eif2c2, Kiaa4215;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12526743; DOI=10.1016/S0960-9822(02)01394-5;
Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.;
"Short-interfering-RNA-mediated gene silencing in mammalian cells
requires Dicer and eIF2C translation initiation factors.";
Curr. Biol. 13:41-46(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
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 158-860.
TISSUE=Embryonic tail;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15284456; DOI=10.1126/science.1102513;
Liu J., Carmell M.A., Rivas F.V., Marsden C.G., Thomson J.M.,
Song J.-J., Hammond S.M., Joshua-Tor L., Hannon G.J.;
"Argonaute2 is the catalytic engine of mammalian RNAi.";
Science 305:1437-1441(2004).
[5]
INTERACTION WITH DICER1 AND TARBP2.
PubMed=16357216; DOI=10.1101/gad.1384005;
Maniataki E., Mourelatos Z.;
"A human, ATP-independent, RISC assembly machine fueled by pre-
miRNA.";
Genes Dev. 19:2979-2990(2005).
[6]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-2, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
Squier T.C., Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to
neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[7]
FUNCTION.
PubMed=17626790; DOI=10.1101/gad.1565607;
O'Carroll D., Mecklenbrauker I., Das P.P., Santana A., Koenig U.,
Enright A.J., Miska E.A., Tarakhovsky A.;
"A Slicer-independent role for Argonaute 2 in hematopoiesis and the
microRNA pathway.";
Genes Dev. 21:1999-2004(2007).
[8]
FUNCTION.
PubMed=19174539; DOI=10.1101/gad.1749809;
Su H., Trombly M.I., Chen J., Wang X.;
"Essential and overlapping functions for mammalian Argonautes in
microRNA silencing.";
Genes Dev. 23:304-317(2009).
[9]
INTERACTION WITH TRIM71.
PubMed=19898466; DOI=10.1038/ncb1987;
Rybak A., Fuchs H., Hadian K., Smirnova L., Wulczyn E.A., Michel G.,
Nitsch R., Krappmann D., Wulczyn F.G.;
"The let-7 target gene mouse lin-41 is a stem cell specific E3
ubiquitin ligase for the miRNA pathway protein Ago2.";
Nat. Cell Biol. 11:1411-1420(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
INTERACTION WITH TRIM71.
PubMed=22508726; DOI=10.1101/gad.187641.112;
Chen J., Lai F., Niswander L.;
"The ubiquitin ligase mLin41 temporally promotes neural progenitor
cell maintenance through FGF signaling.";
Genes Dev. 26:803-815(2012).
[12]
INTERACTION WITH TRIM71.
PubMed=22735451; DOI=10.1038/ncomms1909;
Chang H.M., Martinez N.J., Thornton J.E., Hagan J.P., Nguyen K.D.,
Gregory R.I.;
"Trim71 cooperates with microRNAs to repress Cdkn1a expression and
promote embryonic stem cell proliferation.";
Nat. Commun. 3:923-923(2012).
-!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the
RNA-induced silencing complex (RISC). The 'minimal RISC' appears
to include AGO2 bound to a short guide RNA such as a microRNA
(miRNA) or short interfering RNA (siRNA). These guide RNAs direct
RISC to complementary mRNAs that are targets for RISC-mediated
gene silencing. The precise mechanism of gene silencing depends on
the degree of complementarity between the miRNA or siRNA and its
target. Binding of RISC to a perfectly complementary mRNA
generally results in silencing due to endonucleolytic cleavage of
the mRNA specifically by AGO2. Binding of RISC to a partially
complementary mRNA results in silencing through inhibition of
translation, and this is independent of endonuclease activity. May
inhibit translation initiation by binding to the 7-methylguanosine
cap, thereby preventing the recruitment of the translation
initiation factor eIF4-E. May also inhibit translation initiation
via interaction with EIF6, which itself binds to the 60S ribosomal
subunit and prevents its association with the 40S ribosomal
subunit. The inhibition of translational initiation leads to the
accumulation of the affected mRNA in cytoplasmic processing bodies
(P-bodies), where mRNA degradation may subsequently occur. In some
cases RISC-mediated translational repression is also observed for
miRNAs that perfectly match the 3' untranslated region (3'-UTR).
Can also up-regulate the translation of specific mRNAs under
certain growth conditions. Binds to the AU element of the 3'-UTR
of the TNF (TNF-alpha) mRNA and up-regulates translation under
conditions of serum starvation. Also required for transcriptional
gene silencing (TGS), in which short RNAs known as antigene RNAs
or agRNAs direct the transcriptional repression of complementary
promoter regions. Regulates lymphoid and erythroid development and
function, and this is independent of endonuclease activity.
{ECO:0000255|HAMAP-Rule:MF_03031, ECO:0000269|PubMed:15284456,
ECO:0000269|PubMed:17626790, ECO:0000269|PubMed:19174539}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with DICER1 through its Piwi domain and with
TARBP2 during assembly of the RNA-induced silencing complex
(RISC). Together, DICER1, AGO2 and TARBP2 constitute the trimeric
RISC loading complex (RLC), or micro-RNA (miRNA) loading complex
(miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to
process precursor miRNAs (pre-miRNAs) to mature miRNAs and then
load them onto AGO2. AGO2 bound to the mature miRNA constitutes
the minimal RISC and may subsequently dissociate from DICER1 and
TARBP2. Note however that the term RISC has also been used to
describe the trimeric RLC/miRLC. The formation of RISC complexes
containing siRNAs rather than miRNAs appears to occur
independently of DICER1 (PubMed:16357216). Interacts with AGO1.
Also interacts with DDB1, DDX5, DDX6, DDX20, DHX30, DHX36, DDX47,
DHX9, ELAVL, FXR1, GEMIN4, HNRNPF, IGF2BP1, ILF3, IMP8, MATR3,
PABPC1, PRMT5, P4HA1, P4HB, RBM4, SART3, TNRC6A, TNRC6B, UPF1 and
YBX1. Interacts with the P-body components DCP1A and XRN1.
Associates with polysomes and messenger ribonucleoproteins
(mNRPs). Interacts with RBM4; the interaction is modulated under
stress-induced conditions, occurs under both cell proliferation
and differentiation conditions and in an RNA- and phosphorylation-
independent manner. Interacts with LIMD1, WTIP and AJUBA (By
similarity). Interacts with TRIM71 (PubMed:19898466,
PubMed:22508726, PubMed:22735451). Interacts with APOBEC3G in an
RNA-dependent manner. Interacts with APOBEC3A, APOBEC3C, APOBEC3F
and APOBEC3H. Interacts with DICER1, TARBP2, EIF6, MOV10 and RPL7A
(60S ribosome subunit); they form a large RNA-induced silencing
complex (RISC). Interacts with FMR1. Interacts with ZFP36 (By
similarity). {ECO:0000255|HAMAP-Rule:MF_03031,
ECO:0000269|PubMed:16357216, ECO:0000269|PubMed:19898466,
ECO:0000269|PubMed:22508726, ECO:0000269|PubMed:22735451}.
-!- INTERACTION:
Q9UPY3:DICER1 (xeno); NbExp=2; IntAct=EBI-528299, EBI-395506;
P04156:PRNP (xeno); NbExp=2; IntAct=EBI-528299, EBI-977302;
P04273:PRNP (xeno); NbExp=2; IntAct=EBI-528299, EBI-986426;
Q4VGL6:Rc3h1; NbExp=2; IntAct=EBI-528299, EBI-2366263;
Q9HCJ0:TNRC6C (xeno); NbExp=3; IntAct=EBI-528299, EBI-6507625;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000255|HAMAP-
Rule:MF_03031}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03031}.
Note=Translational repression of mRNAs results in their
recruitment to P-bodies. Translocation to the nucleus requires
IMP8. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- TISSUE SPECIFICITY: Ubiquitous expression in 9.5 day embryos with
highest levels in forebrain, heart, limb buds, and branchial
arches. {ECO:0000269|PubMed:15284456}.
-!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism
similar to that of RNase H. However, while RNase H utilizes a
triad of Asp-Asp-Glu (DDE) for metal ion coordination, this
protein appears to utilize a triad of Asp-Asp-His (DDH).
{ECO:0000255|HAMAP-Rule:MF_03031}.
-!- PTM: Hydroxylated. 4-hydroxylation appears to enhance protein
stability but is not required for miRNA-binding or endonuclease
activity. {ECO:0000255|HAMAP-Rule:MF_03031}.
-!- DISRUPTION PHENOTYPE: Embryonic death with a strong defect in
neural tube closure and apparent cardiac failure.
{ECO:0000269|PubMed:15284456}.
-!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
{ECO:0000255|HAMAP-Rule:MF_03031}.
-!- SEQUENCE CAUTION:
Sequence=AAH96465.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB081472; BAC15767.1; -; mRNA.
EMBL; BC096465; AAH96465.1; ALT_INIT; mRNA.
EMBL; BC128379; AAI28380.1; -; mRNA.
EMBL; BC129922; AAI29923.1; -; mRNA.
EMBL; AK220193; BAD90378.1; -; mRNA.
CCDS; CCDS37098.1; -.
RefSeq; NP_694818.3; NM_153178.4.
UniGene; Mm.23095; -.
UniGene; Mm.391971; -.
UniGene; Mm.440409; -.
UniGene; Mm.476931; -.
UniGene; Mm.486474; -.
UniGene; Mm.490340; -.
ProteinModelPortal; Q8CJG0; -.
SMR; Q8CJG0; -.
BioGrid; 232092; 7.
DIP; DIP-35014N; -.
IntAct; Q8CJG0; 53.
STRING; 10090.ENSMUSP00000042207; -.
iPTMnet; Q8CJG0; -.
PhosphoSitePlus; Q8CJG0; -.
EPD; Q8CJG0; -.
MaxQB; Q8CJG0; -.
PaxDb; Q8CJG0; -.
PeptideAtlas; Q8CJG0; -.
PRIDE; Q8CJG0; -.
Ensembl; ENSMUST00000044113; ENSMUSP00000042207; ENSMUSG00000036698.
GeneID; 239528; -.
KEGG; mmu:239528; -.
UCSC; uc007wbu.2; mouse.
CTD; 27161; -.
MGI; MGI:2446632; Ago2.
eggNOG; KOG1041; Eukaryota.
eggNOG; ENOG410XP07; LUCA.
GeneTree; ENSGT00760000119148; -.
HOGENOM; HOG000116043; -.
HOVERGEN; HBG006101; -.
InParanoid; Q8CJG0; -.
KO; K11593; -.
OMA; SPDGYYH; -.
OrthoDB; EOG091G020J; -.
TreeFam; TF101510; -.
Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
Reactome; R-MMU-426496; Post-transcriptional silencing by small RNAs.
Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
PRO; PR:Q8CJG0; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000036698; -.
CleanEx; MM_EIF2C2; -.
Genevisible; Q8CJG0; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:MGI.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0000932; C:P-body; IDA:MGI.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:0016442; C:RISC complex; IDA:BHF-UCL.
GO; GO:0070578; C:RISC-loading complex; IDA:BHF-UCL.
GO; GO:0001047; F:core promoter binding; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0004521; F:endoribonuclease activity; IDA:MGI.
GO; GO:0090624; F:endoribonuclease activity, cleaving miRNA-paired mRNA; ISO:MGI.
GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035198; F:miRNA binding; IDA:MGI.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:0098808; F:mRNA cap binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0000993; F:RNA polymerase II core binding; ISO:MGI.
GO; GO:0003727; F:single-stranded RNA binding; ISO:MGI.
GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
GO; GO:0035280; P:miRNA loading onto RISC involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0035278; P:miRNA mediated inhibition of translation; ISS:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0090625; P:mRNA cleavage involved in gene silencing by siRNA; ISO:MGI.
GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:1905618; P:positive regulation of miRNA mediated inhibition of translation; ISO:MGI.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0031054; P:pre-miRNA processing; IDA:BHF-UCL.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; IMP:MGI.
GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
GO; GO:0035087; P:siRNA loading onto RISC involved in RNA interference; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_03031; AGO2; 1.
InterPro; IPR028602; AGO2.
InterPro; IPR014811; ArgoL1.
InterPro; IPR032472; ArgoL2.
InterPro; IPR032473; Argonaute_Mid_dom.
InterPro; IPR032474; Argonaute_N.
InterPro; IPR003100; PAZ_dom.
InterPro; IPR036085; PAZ_dom_sf.
InterPro; IPR003165; Piwi.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF08699; ArgoL1; 1.
Pfam; PF16488; ArgoL2; 1.
Pfam; PF16487; ArgoMid; 1.
Pfam; PF16486; ArgoN; 1.
Pfam; PF02170; PAZ; 1.
Pfam; PF02171; Piwi; 1.
SMART; SM01163; DUF1785; 1.
SMART; SM00949; PAZ; 1.
SMART; SM00950; Piwi; 1.
SUPFAM; SSF101690; SSF101690; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50821; PAZ; 1.
PROSITE; PS50822; PIWI; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Endonuclease; Hydrolase; Hydroxylation; Magnesium; Manganese;
Metal-binding; Nitration; Nuclease; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Transcription; Transcription regulation;
Translation regulation.
CHAIN 1 860 Protein argonaute-2.
/FTId=PRO_0000194058.
DOMAIN 236 349 PAZ. {ECO:0000255|HAMAP-Rule:MF_03031}.
DOMAIN 518 819 Piwi. {ECO:0000255|HAMAP-Rule:MF_03031}.
REGION 312 317 Interaction with guide RNA.
{ECO:0000250}.
REGION 525 567 Interaction with guide RNA.
{ECO:0000250}.
REGION 588 591 Interaction with GW182 family members.
{ECO:0000255}.
REGION 651 661 Interaction with GW182 family members.
{ECO:0000255}.
REGION 710 711 Interaction with guide RNA.
{ECO:0000250}.
REGION 754 762 Interaction with guide RNA.
{ECO:0000250}.
REGION 791 813 Interaction with guide RNA.
{ECO:0000250}.
METAL 598 598 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_03031}.
METAL 670 670 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_03031}.
METAL 808 808 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_03031}.
MOD_RES 2 2 Nitrated tyrosine.
{ECO:0000244|PubMed:16800626}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKV8}.
MOD_RES 701 701 4-hydroxyproline. {ECO:0000255|HAMAP-
Rule:MF_03031}.
MOD_RES 829 829 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKV8}.
CONFLICT 65 65 E -> G (in Ref. 2; AAH96465).
{ECO:0000305}.
CONFLICT 67 67 C -> R (in Ref. 1; BAC15767).
{ECO:0000305}.
CONFLICT 129 129 F -> L (in Ref. 1; BAC15767).
{ECO:0000305}.
CONFLICT 360 360 N -> D (in Ref. 1; BAC15767).
{ECO:0000305}.
CONFLICT 563 563 N -> D (in Ref. 2; AAH96465).
{ECO:0000305}.
CONFLICT 711 711 R -> P (in Ref. 2; AAH96465).
{ECO:0000305}.
CONFLICT 761 761 S -> G (in Ref. 1; BAC15767).
{ECO:0000305}.
SEQUENCE 860 AA; 97304 MW; A4E13C633846062C CRC64;
MYSGAGPVLA SPAPTTSPIP GYAFKPPPRP DFGTTGRTIK LQANFFEMDI PKIDIYHYEL
DIKPEKCPRR VNREIVEHMV QHFKTQIFGD RKPVFDGRKN LYTAMPLPIG RDKVELEVTL
PGEGKDRIFK VSIKWVSCVS LQALHDALSG RLPSVPFETI QALDVVMRHL PSMRYTPVGR
SFFTASEGCS NPLGGGREVW FGFHQSVRPS LWKMMLNIDV SATAFYKAQP VIEFVCEVLD
FKSIEEQQKP LTDSQRVKFT KEIKGLKVEI THCGQMKRKY RVCNVTRRPA SHQTFPLQQE
SGQTVECTVA QYFKDRHKLV LRYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
QTSTMIRATA RSAPDRQEEI SKLMRSASFN TDPYVREFGI MVKDEMTDVT GRVLQPPSIL
YGGRNKAIAT PVQGVWDMRN KQFHTGIEIK VWAIACFAPQ RQCTEVHLKS FTEQLRKISR
DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYAGLQLVV VILPGKTPVY AEVKRVGDTV
LGMATQCVQM KNVQRTTPQT LSNLCLKINV KLGGVNNILL PQGRPPVFQQ PVIFLGADVT
HPPAGDGKKP SIAAVVGSMD AHPNRYCATV RVQQHRQEII QDLAAMVREL LIQFYKSTRF
KPTRIIFYRD GVSEGQFQQV LHHELLAIRE ACIKLEKDYQ PGITFIVVQK RHHTRLFCTD
KNERVGKSGN IPAGTTVDTK ITHPTEFDFY LCSHAGIQGT SRPSHYHVLW DDNRFSSDEL
QILTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH TSGQSNGRDH
QALAKAVQVH QDTLRTMYFA


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18-003-42779 Probable ATP-dependent RNA helicase DDX48 - EC 3.6.1.-; DEAD box protein 48; Eukaryotic initiation factor 4A-like NUK-34; Nuclear matrix protein 265; hNMP 265; Eukaryotic translation initiation factor 0.1 mg Protein A
YF-PA26955 Mouse polyclonal to Argonaute 3 _ eIF2C 3, Host Mouse 50 uL
YF-PA22643 Rabbit polyclonal to Argonaute 3 _ eIF2C 3, Host Rabbit 100 ug
CSB-EL007520RA Rat Protein argonaute-2(EIF2C2) ELISA kit 96T
E2027d Mouse ELISA Kit FOR Protein argonaute-4 96T
AGO1_MOUSE Mouse ELISA Kit FOR Protein argonaute-1 96T
E10828r Mouse ELISA Kit FOR Protein argonaute-3 96T
G2411 Protein argonaute-2 (EIF2C2), Rat, ELISA Kit 96T
E10828Rb Chicken ELISA Kit FOR Protein argonaute-4 96T
EIAAB12753 66 kDa tyrosine-rich heat shock protein,67 kDa polymerase-associated factor,Eif3eip,eIF3l,Eif3l,Eif3s6ip,Eukaryotic translation initiation factor 3 subunit 6-interacting protein,Eukaryotic translation
G2418 Protein argonaute-4 (EIF2C4), Mouse, ELISA Kit 96T
CSB-EL007520RA Rat Protein argonaute-2(EIF2C2) ELISA kit SpeciesRat 96T
abx109351 Polyclonal Rabbit Protein argonaute-2 Antibody 100 μg
CSB-EL007521BO Bovine Protein argonaute-3(EIF2C3) ELISA kit 96T
CSB-EL007519MO Mouse Protein argonaute-1(EIF2C1) ELISA kit 96T
CSB-EL007520BO Bovine Protein argonaute-2(EIF2C2) ELISA kit 96T
abx108654 Polyclonal Rabbit Protein argonaute-2 Antibody (HRP) 100 μg
CSB-EL007522CH Chicken Protein argonaute-4(EIF2C4) ELISA kit 96T
CSB-EL007521CH Chicken Protein argonaute-3(EIF2C3) ELISA kit 96T
CSB-EL007519HU Human Protein argonaute-1(EIF2C1) ELISA kit 96T


 

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