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Heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)

 ROA2_RAT                Reviewed;         353 AA.
A7VJC2; A7VJC1; A7VJC3; A7VJC4;
03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 1.
23-MAY-2018, entry version 90.
RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1 {ECO:0000312|EMBL:BAF79676.1};
Short=hnRNP A2/B1;
Name=Hnrnpa2b1 {ECO:0000250|UniProtKB:P22626};
Synonyms=Hnrnp {ECO:0000312|EMBL:BAF79676.1},
Hnrpa2b1 {ECO:0000250|UniProtKB:P22626};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A2; B1; A2B AND B1B), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=9925756; DOI=10.1006/excr.1998.4323;
Kamma H., Horiguchi H., Wan L., Matsui M., Fuiwara M., Fujimoto M.,
Yazawa T., Dreyfuss G.;
"Molecular characterization of the hnRNP A2/B1 proteins: tissue-
specific expression and novel isoforms.";
Exp. Cell Res. 246:399-411(1999).
[2]
PROTEIN SEQUENCE OF 100-113; 116-137 AND 2014-226, FUNCTION,
RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=9578590; DOI=10.1021/bi9800247;
Hoek K.S., Kidd G.J., Carson J.H., Smith R.;
"hnRNP A2 selectively binds the cytoplasmic transport sequence of
myelin basic protein mRNA.";
Biochemistry 37:7021-7029(1998).
[3]
FUNCTION, AND RNA-BINDING.
PubMed=10567417; DOI=10.1074/jbc.274.48.34389;
Munro T.P., Magee R.J., Kidd G.J., Carson J.H., Barbarese E.,
Smith L.M., Smith R.;
"Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2
response element for RNA trafficking.";
J. Biol. Chem. 274:34389-34395(1999).
[4]
METHYLATION.
PubMed=10772824; DOI=10.1006/excr.2000.4827;
Nichols R.C., Wang X.W., Tang J., Hamilton B.J., High F.A.,
Herschman H.R., Rigby W.F.;
"The RGG domain in hnRNP A2 affects subcellular localization.";
Exp. Cell Res. 256:522-532(2000).
[5]
FUNCTION.
PubMed=15659580; DOI=10.1093/nar/gki203;
Moran-Jones K., Wayman L., Kennedy D.D., Reddel R.R., Sara S.,
Snee M.J., Smith R.;
"hnRNP A2, a potential ssDNA/RNA molecular adapter at the telomere.";
Nucleic Acids Res. 33:486-496(2005).
[6]
REVIEW.
PubMed=19099192; DOI=10.1007/s00018-008-8532-1;
He Y., Smith R.;
"Nuclear functions of heterogeneous nuclear ribonucleoproteins A/B.";
Cell. Mol. Life Sci. 66:1239-1256(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=19343716; DOI=10.1002/pmic.200800664;
Maurya D.K., Sundaram C.S., Bhargava P.;
"Proteome profile of the mature rat olfactory bulb.";
Proteomics 9:2593-2599(2009).
[8]
SUBCELLULAR LOCATION (ISOFORMS B1; A2; A2B AND B1B).
PubMed=20406423; DOI=10.1111/j.1600-0854.2010.01072.x;
Han S.P., Friend L.R., Carson J.H., Korza G., Barbarese E.,
Maggipinto M., Hatfield J.T., Rothnagel J.A., Smith R.;
"Differential subcellular distributions and trafficking functions of
hnRNP A2/B1 spliceoforms.";
Traffic 11:886-898(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-259 AND
SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[10]
ACETYLATION AT MET-1, METHYLATION AT ARG-266, SUBCELLULAR LOCATION
(ISOFORM A2), AND MUTAGENESIS OF ARG-266.
PubMed=24098712; DOI=10.1371/journal.pone.0075669;
Friend L.R., Landsberg M.J., Nouwens A.S., Wei Y., Rothnagel J.A.,
Smith R.;
"Arginine methylation of hnRNP A2 does not directly govern its
subcellular localization.";
PLoS ONE 8:E75669-E75669(2013).
-!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that
associates with nascent pre-mRNAs, packaging them into hnRNP
particles. The hnRNP particle arrangement on nascent hnRNA is non-
random and sequence-dependent and serves to condense and stabilize
the transcripts and minimize tangling and knotting. Packaging
plays a role in various processes such as transcription, pre-mRNA
processing, RNA nuclear export, subcellular location, mRNA
translation and stability of mature mRNAs. Forms hnRNP particles
with at least 20 other different hnRNP and heterogeneous nuclear
RNA in the nucleus (PubMed:19099192). Involved in transport of
specific mRNAs to the cytoplasm in oligodendrocytes and neurons:
acts by specifically recognizing and binding the A2RE (21
nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11
nucleotide oligonucleotide) sequence motifs present on some mRNAs,
and promotes their transport to the cytoplasm (PubMed:9578590,
PubMed:10567417). Specifically binds single-stranded telomeric DNA
sequences, protecting telomeric DNA repeat against endonuclease
digestion (PubMed:15659580). Also binds other RNA molecules, such
as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the
N6-methyladenosine (m6A) mark by specifically recognizing and
binding a subset of nuclear m6A-containing pri-miRNAs. Binding to
m6A-containing pri-miRNAs promotes pri-miRNA processing by
enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in
miRNA sorting into exosomes following sumoylation, possibly by
binding (m6A)-containing pre-miRNAs. Acts as a regulator of
efficiency of mRNA splicing, possibly by binding to m6A-containing
pre-mRNAs (By similarity). {ECO:0000250|UniProtKB:P22626,
ECO:0000269|PubMed:10567417, ECO:0000269|PubMed:15659580,
ECO:0000269|PubMed:9578590, ECO:0000303|PubMed:19099192}.
-!- SUBUNIT: Identified in the spliceosome C complex. Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs. Interacts with IGF2BP1. Interacts with C9orf72. Interacts
with DGCR8. Interacts with TARDBP. Interacts with CKAP5.
{ECO:0000250|UniProtKB:P22626}.
-!- SUBCELLULAR LOCATION: Isoform B1: Nucleus
{ECO:0000269|PubMed:20406423}.
-!- SUBCELLULAR LOCATION: Isoform A2: Nucleus
{ECO:0000269|PubMed:20406423, ECO:0000269|PubMed:24098712}.
-!- SUBCELLULAR LOCATION: Isoform A2b: Cytoplasm
{ECO:0000269|PubMed:20406423}. Nucleus
{ECO:0000269|PubMed:20406423}. Note=Mainly localizes in the
cytoplasm in neural cells. {ECO:0000269|PubMed:20406423}.
-!- SUBCELLULAR LOCATION: Isoform B1b: Cytoplasm
{ECO:0000269|PubMed:20406423}. Nucleus
{ECO:0000269|PubMed:20406423}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:9578590, ECO:0000269|PubMed:9925756}.
Cytoplasm {ECO:0000269|PubMed:9925756}. Cytoplasmic granule
{ECO:0000250|UniProtKB:P22626}. Secreted, exosome
{ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs. Component of
ribonucleosomes. Not found in the nucleolus. Found in exosomes
follwong sumoylation. {ECO:0000250|UniProtKB:P22626}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.
{ECO:0000269|PubMed:9925756};
Name=B1 {ECO:0000303|PubMed:9925756};
IsoId=A7VJC2-1; Sequence=Displayed;
Name=A2 {ECO:0000303|PubMed:9925756};
IsoId=A7VJC2-2; Sequence=VSP_053031;
Name=A2b; Synonyms=B0a {ECO:0000303|PubMed:9925756};
IsoId=A7VJC2-3; Sequence=VSP_053031, VSP_053032;
Name=B1b; Synonyms=B0b {ECO:0000303|PubMed:9925756};
IsoId=A7VJC2-4; Sequence=VSP_053032;
-!- TISSUE SPECIFICITY: In the brain, isoform A2 and isoform B1 are
abundant in large ganglion-type neurons, such as Purkinje cells,
and are less abundant in neighboring glia cells. Isoform A2 is
more abundant than isoform B1 in brain. In testis, isoform A2 and
isoform B1 are present in spermatogonia and spermatocytes, but not
in spermatids or sperm. Isoform A2 is more abundant in the adrenal
medulla than in the cortical cells. Isoform B1 is found in both
adrenal medulla and cortical cells. Isoform A2 is more abundant
than isoform B1 in the adrenal gland. Isoform A2 and isoform B1
are both detected in pancreas and kidney, and at lower levels in
heart and lung. Isoform B1 is more abundant than isoform A2 in
heart, lung and intestine (at protein level). Isoform A2b and
isoform B1b are testis-specific. {ECO:0000269|PubMed:9925756}.
-!- DOMAIN: The low complexity (LC) region is intrinsically
disordered. When incubated at high concentration, it is able to
polymerize into labile, amyloid-like fibers and form cross-beta
polymerization structures, probably driving the formation of
hydrogels. In contrast to irreversible, pathogenic amyloids, the
fibers polymerized from LC regions disassemble upon dilution. A
number of evidences suggest that formation of cross-beta
structures by LC regions mediate the formation of RNA granules,
liquid-like droplets, and hydrogels.
{ECO:0000250|UniProtKB:P22626}.
-!- PTM: Asymmetric dimethylation at Arg-266 constitutes the major
methylation site (PubMed:24098712). According to a report,
methylation affects subcellular location and promotes nuclear
localization (PubMed:10772824). According to another report,
methylation at Arg-266 does not influence nucleocytoplasmic
shuttling (PubMed:24098712). {ECO:0000269|PubMed:10772824,
ECO:0000269|PubMed:24098712}.
-!- PTM: Sumoylated in exosomes, promoting miRNAs-binding.
{ECO:0000250|UniProtKB:P22626}.
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EMBL; AB006815; BAF79675.1; -; mRNA.
EMBL; AB006816; BAF79676.1; -; mRNA.
EMBL; AB006817; BAF79677.1; -; mRNA.
EMBL; AB006818; BAF79678.1; -; mRNA.
RefSeq; NP_001098083.1; NM_001104613.1. [A7VJC2-1]
UniGene; Rn.233238; -.
UniGene; Rn.4057; -.
ProteinModelPortal; A7VJC2; -.
SMR; A7VJC2; -.
BioGrid; 263391; 2.
IntAct; A7VJC2; 1.
STRING; 10116.ENSRNOP00000015152; -.
iPTMnet; A7VJC2; -.
SwissPalm; A7VJC2; -.
PaxDb; A7VJC2; -.
PeptideAtlas; A7VJC2; -.
PRIDE; A7VJC2; -.
GeneID; 362361; -.
KEGG; rno:362361; -.
UCSC; RGD:1310403; rat. [A7VJC2-1]
CTD; 3181; -.
RGD; 1310403; Hnrnpa2b1.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
HOGENOM; HOG000234442; -.
HOVERGEN; HBG108415; -.
InParanoid; A7VJC2; -.
KO; K13158; -.
PhylomeDB; A7VJC2; -.
PRO; PR:A7VJC2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
GO; GO:0000785; C:chromatin; IDA:RGD.
GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:RGD.
GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:1990715; F:mRNA CDS binding; IDA:RGD.
GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
GO; GO:0001069; F:regulatory region RNA binding; IDA:RGD.
GO; GO:0003723; F:RNA binding; IDA:RGD.
GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:UniProtKB.
GO; GO:0044806; P:G-quadruplex DNA unwinding; IDA:BHF-UCL.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:1990428; P:miRNA transport; ISS:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
GO; GO:1905663; P:positive regulation of telomerase RNA reverse transcriptase activity; IDA:BHF-UCL.
GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IDA:BHF-UCL.
GO; GO:0031053; P:primary miRNA processing; ISS:UniProtKB.
GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
GO; GO:0050658; P:RNA transport; IMP:RGD.
GO; GO:0016233; P:telomere capping; IDA:UniProtKB.
CDD; cd12762; RRM1_hnRNPA2B1; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR034489; hnRNP_A2/B1.
InterPro; IPR034486; hnRNPA2B1_RRM1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR44531; PTHR44531; 1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Methylation;
mRNA processing; mRNA splicing; mRNA transport; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
RNA-binding; Secreted; Spliceosome; Transport; Ubl conjugation.
CHAIN 1 353 Heterogeneous nuclear ribonucleoproteins
A2/B1.
/FTId=PRO_0000365101.
DOMAIN 21 104 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 112 191 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 193 353 Low complexity (LC) region.
{ECO:0000269|PubMed:24098712}.
REGION 308 347 Nuclear targeting sequence.
{ECO:0000250|UniProtKB:P22626}.
MOTIF 9 15 Nuclear localization signal.
{ECO:0000250|UniProtKB:P22626,
ECO:0000255}.
COMPBIAS 202 349 Gly-rich. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:24098712}.
MOD_RES 4 4 Phosphothreonine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 38 38 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O88569}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 104 104 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 159 159 Phosphothreonine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 168 168 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 173 173 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 176 176 Phosphothreonine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 203 203 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:O88569}.
MOD_RES 203 203 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 203 203 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 213 213 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:O88569}.
MOD_RES 213 213 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 213 213 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 228 228 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 238 238 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 266 266 Asymmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:24098712}.
MOD_RES 266 266 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 325 325 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 331 331 Phosphotyrosine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 347 347 Phosphotyrosine.
{ECO:0000250|UniProtKB:P22626}.
MOD_RES 350 350 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 137 137 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 168 168 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 173 173 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P22626}.
CROSSLNK 186 186 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P22626}.
VAR_SEQ 3 14 Missing (in isoform A2 and isoform A2b).
{ECO:0000303|PubMed:9925756}.
/FTId=VSP_053031.
VAR_SEQ 254 293 Missing (in isoform A2b and isoform B1b).
{ECO:0000303|PubMed:9925756}.
/FTId=VSP_053032.
MUTAGEN 266 266 R->A: Decreased methylation. Does not
affect subcellular location.
{ECO:0000269|PubMed:24098712}.
SEQUENCE 353 AA; 37478 MW; 1C2E7BA8C8E98D6E CRC64;
MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIF LQKYHTINGH
NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGNY
NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY


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25-629 HNRPDL belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) 0.05 mg
29-477 HNRPC belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). 0.05 mg
29-296 PTBP1 belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). 0.05 mg
29-353 HNRPDL belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA) 0.1 mg
29-284 HNRPK belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). 0.05 mg
25-608 PTBP1 belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). 0.05 mg
29-283 HNRPK belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). 0.1 mg
29-229 HNRPD belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA 0.1 mg
29-228 HNRPD belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA 0.1 mg
29-281 HNRPA1 belongs to the A_B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hn 0.1 mg
29-282 HNRPA1 belongs to the A_B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hn 0.1 mg


 

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