Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

High mobility group protein HMG-I/HMG-Y (HMG-I(Y)) (High mobility group AT-hook protein 1) (High mobility group protein A1)

 HMGA1_MOUSE             Reviewed;         107 AA.
P17095; Q91WV2; Q924L7; Q924L8;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
31-JAN-2018, entry version 174.
RecName: Full=High mobility group protein HMG-I/HMG-Y;
Short=HMG-I(Y);
AltName: Full=High mobility group AT-hook protein 1;
Short=High mobility group protein A1;
Name=Hmga1; Synonyms=Hmgi, Hmgiy;
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] (ISOFORM HMG-Y).
PubMed=3192537;
Johnson K.R., Lehn D.A., Elton T.S., Barr P.J., Reeves R.;
"Complete murine cDNA sequence, genomic structure, and tissue
expression of the high mobility group protein HMG-I(Y).";
J. Biol. Chem. 263:18338-18342(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HMG-I AND HMG-Y).
STRAIN=BALB/cJ;
PubMed=11410365; DOI=10.1016/S0378-1119(01)00500-5;
Pedulla M.L., Treff N.R., Resar L.M.S., Reeves R.;
"Sequence and analysis of the murine Hmgiy (Hmga1) gene locus.";
Gene 271:51-58(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HMG-Y).
STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HMG-I).
STRAIN=FVB/N; TISSUE=Colon;
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).
[5]
PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, ACETYLATION AT SER-2,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=1429598;
Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H.,
Manfioletti G., Giancotti V.;
"Mass spectrometric analysis of the HMGY protein from Lewis lung
carcinoma. Identification of phosphorylation sites.";
J. Biol. Chem. 267:22486-22489(1992).
[6]
INTERACTION WITH HIPK2, AND PHOSPHORYLATION.
PubMed=11593421; DOI=10.1038/sj.onc.1204635;
Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R.,
Viglietto G., Santoro M., Chiariotti L., Fusco A.;
"High mobility group I (Y) proteins bind HIPK2, a serine-threonine
kinase protein which inhibits cell growth.";
Oncogene 20:6132-6141(2001).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Teratocarcinoma;
PubMed=17622165; DOI=10.1021/pr070122r;
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19
cells.";
J. Proteome Res. 6:3174-3186(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-99; SER-102 AND
SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-99; SER-102 AND
SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-7 AND LYS-15,
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T
rich regions in double-stranded DNA. It is suggested that these
proteins could function in nucleosome phasing and in the 3'-end
processing of mRNA transcripts. They are also involved in the
transcription regulation of genes containing, or in close
proximity to A+T-rich regions.
-!- SUBUNIT: Interacts with HIPK2. {ECO:0000269|PubMed:11593421}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=HMG-I; Synonyms=HMGA1a;
IsoId=P17095-2; Sequence=Displayed;
Name=HMG-Y; Synonyms=HMGA1b, HMGI-E;
IsoId=P17095-1; Sequence=VSP_012406;
-!- PTM: Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2.
Phosphorylation may modulate DNA-binding affinity (By similarity).
{ECO:0000250}.
-!- PTM: Methylation at Arg-58 is mutually exclusive with methylation
at Arg-60. {ECO:0000250}.
-!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04179; AAA37820.1; -; mRNA.
EMBL; AF285780; AAK66158.1; -; Genomic_DNA.
EMBL; AF285780; AAK66159.1; -; Genomic_DNA.
EMBL; AK010617; BAB27065.1; -; mRNA.
EMBL; BC013455; AAH13455.1; -; mRNA.
CCDS; CCDS28564.1; -. [P17095-2]
CCDS; CCDS49010.1; -. [P17095-2]
CCDS; CCDS50044.1; -. [P17095-1]
PIR; A31895; A31895.
RefSeq; NP_001020598.1; NM_001025427.3. [P17095-2]
RefSeq; NP_001034445.1; NM_001039356.2. [P17095-2]
RefSeq; NP_001159948.1; NM_001166476.1. [P17095-2]
RefSeq; NP_001159949.1; NM_001166477.1. [P17095-1]
RefSeq; NP_001160007.1; NM_001166535.1. [P17095-2]
RefSeq; NP_001160008.1; NM_001166536.1. [P17095-2]
RefSeq; NP_001160009.1; NM_001166537.1. [P17095-1]
RefSeq; NP_001160011.1; NM_001166539.1. [P17095-1]
RefSeq; NP_001160012.1; NM_001166540.1. [P17095-1]
RefSeq; NP_001160013.1; NM_001166541.1. [P17095-1]
RefSeq; NP_001160014.1; NM_001166542.1. [P17095-1]
RefSeq; NP_057869.2; NM_016660.3. [P17095-2]
UniGene; Mm.426212; -.
UniGene; Mm.440289; -.
UniGene; Mm.4438; -.
ProteinModelPortal; P17095; -.
BioGrid; 200340; 8.
DIP; DIP-53N; -.
IntAct; P17095; 4.
MINT; MINT-1848156; -.
STRING; 10090.ENSMUSP00000113011; -.
iPTMnet; P17095; -.
PhosphoSitePlus; P17095; -.
EPD; P17095; -.
PaxDb; P17095; -.
PeptideAtlas; P17095; -.
PRIDE; P17095; -.
TopDownProteomics; P17095-1; -. [P17095-1]
TopDownProteomics; P17095-2; -. [P17095-2]
Ensembl; ENSMUST00000105046; ENSMUSP00000100667; ENSMUSG00000078249. [P17095-2]
Ensembl; ENSMUST00000114888; ENSMUSP00000110538; ENSMUSG00000046711. [P17095-1]
Ensembl; ENSMUST00000117254; ENSMUSP00000113011; ENSMUSG00000046711. [P17095-2]
Ensembl; ENSMUST00000117600; ENSMUSP00000113068; ENSMUSG00000046711. [P17095-2]
Ensembl; ENSMUST00000118570; ENSMUSP00000114101; ENSMUSG00000046711. [P17095-1]
Ensembl; ENSMUST00000118599; ENSMUSP00000113015; ENSMUSG00000046711. [P17095-2]
Ensembl; ENSMUST00000119486; ENSMUSP00000113916; ENSMUSG00000046711. [P17095-2]
GeneID; 111241; -.
GeneID; 15361; -.
KEGG; mmu:111241; -.
KEGG; mmu:15361; -.
UCSC; uc008boz.2; mouse. [P17095-2]
CTD; 111241; -.
CTD; 3159; -.
MGI; MGI:96160; Hmga1.
eggNOG; ENOG410J4ZT; Eukaryota.
eggNOG; ENOG410Z566; LUCA.
GeneTree; ENSGT00730000111329; -.
HOGENOM; HOG000076308; -.
HOVERGEN; HBG063451; -.
InParanoid; P17095; -.
KO; K09282; -.
OMA; NMSDKGT; -.
PhylomeDB; P17095; -.
TreeFam; TF351623; -.
Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
PRO; PR:P17095; -.
Proteomes; UP000000589; Chromosome 11.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000046711; -.
CleanEx; MM_HMGA1; -.
ExpressionAtlas; P17095; baseline and differential.
Genevisible; P17095; MM.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0035985; C:senescence-associated heterochromatin focus; ISS:UniProtKB.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISO:MGI.
GO; GO:0003680; F:AT DNA binding; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IDA:BHF-UCL.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; ISO:MGI.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISS:UniProtKB.
GO; GO:0042974; F:retinoic acid receptor binding; ISS:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0090402; P:oncogene-induced cell senescence; ISS:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0035986; P:senescence-associated heterochromatin focus assembly; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
InterPro; IPR017956; AT_hook_DNA-bd_motif.
InterPro; IPR000116; HMGA.
InterPro; IPR031079; HMGA1_mammal.
InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
PANTHER; PTHR23341:SF1; PTHR23341:SF1; 1.
PRINTS; PR00929; ATHOOK.
PRINTS; PR00930; HIGHMOBLTYIY.
SMART; SM00384; AT_hook; 3.
PROSITE; PS00354; HMGI_Y; 3.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Alternative splicing; Chromosome;
Complete proteome; DNA-binding; Isopeptide bond; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337,
ECO:0000269|PubMed:1429598}.
CHAIN 2 107 High mobility group protein HMG-I/HMG-Y.
/FTId=PRO_0000206709.
DNA_BIND 21 31 A.T hook 1.
DNA_BIND 53 63 A.T hook 2.
DNA_BIND 78 89 A.T hook 3.
REGION 53 77 Interaction with HIPK2.
{ECO:0000269|PubMed:11593421}.
COMPBIAS 91 106 Glu-rich (acidic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:23806337,
ECO:0000269|PubMed:1429598}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 8 8 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 9 9 ADP-ribosylserine; alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 9 9 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 26 26 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 26 26 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 26 26 Symmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 36 36 Phosphoserine; by HIPK2 and CDC2.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 53 53 Phosphothreonine; by HIPK2 and CDC2.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 58 58 Asymmetric dimethylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 58 58 Omega-N-methylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 60 60 Asymmetric dimethylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 60 60 Omega-N-methylarginine; by PRMT6;
alternate.
{ECO:0000250|UniProtKB:P17096}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1429598}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1429598}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17622165,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1429598}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P17096}.
VAR_SEQ 35 45 Missing (in isoform HMG-Y).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:3192537}.
/FTId=VSP_012406.
CONFLICT 106 106 E -> G (in Ref. 2; AAK66158/AAK66159).
{ECO:0000305}.
SEQUENCE 107 AA; 11614 MW; 4EC39386611959FC CRC64;
MSESGSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGAA KTRKVTTAPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ


Related products :

Catalog number Product name Quantity
18-003-43339 High mobility group protein HMGI-C - High mobility group AT-hook protein 2 Polyclonal 0.1 mg Protein A
E0399r ELISA Amphoterin,Heparin-binding protein p30,High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Rat,Rattus norvegicus 96T
E0399r ELISA kit Amphoterin,Heparin-binding protein p30,High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Rat,Rattus norvegicus 96T
U0399r CLIA Amphoterin,Heparin-binding protein p30,High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Rat,Rattus norvegicus 96T
EIAAB43466 Homo sapiens,Human,KIAA0808,Thymocyte selection-associated high mobility group box protein TOX,Thymus high mobility group box protein TOX,TOX
U0399h CLIA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Homo sapiens,Human 96T
E0399h ELISA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Homo sapiens,Human 96T
E0399h ELISA kit High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Homo sapiens,Human 96T
E0399b ELISA kit Bos taurus,Bovine,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
E0399m ELISA High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Mouse,Mus musculus 96T
U0399m CLIA High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Mouse,Mus musculus 96T
U0399b CLIA Bos taurus,Bovine,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
EIAAB43465 Mouse,Mus musculus,Thymocyte selection-associated high mobility group box protein TOX,Thymus high mobility group box protein TOX,Tox
E0399m ELISA kit High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Mouse,Mus musculus 96T
E0399b ELISA Bos taurus,Bovine,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
E0399p ELISA kit High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Pig,Sus scrofa 96T
U0399p CLIA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Pig,Sus scrofa 96T
E0399p ELISA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Pig,Sus scrofa 96T
orb82706 Human HMG His tag protein Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 oramphoterin, is a member of the high mobility group box family of non-histonechromosomal proteins. 1 mg
18-003-42695 High mobility group protein B3 - High mobility group protein 4; HMG-4; High mobility group protein 2a; HMG-2a Polyclonal 0.1 mg Protein A
18-003-42696 High mobility group protein B3 - High mobility group protein 4; HMG-4; High mobility group protein 2a; HMG-2a Polyclonal 0.1 mg Protein A
126-10094 Goat Anti-High-Mobility Group Box 3 (HMGB3) + High-Mobility Group Box 4 (HMG4), with HRP-conjugated secondary antibody 100
U0399c CLIA Chicken,Gallus gallus,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
E0399c ELISA kit Chicken,Gallus gallus,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
E0399c ELISA Chicken,Gallus gallus,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur