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Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)

 GRP75_MOUSE             Reviewed;         679 AA.
P38647; Q3TW93; Q3UVN1; Q3V015; Q7TSZ0; Q9CQ05;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
22-NOV-2017, entry version 170.
RecName: Full=Stress-70 protein, mitochondrial;
AltName: Full=75 kDa glucose-regulated protein;
Short=GRP-75;
AltName: Full=Heat shock 70 kDa protein 9;
AltName: Full=Mortalin;
AltName: Full=Peptide-binding protein 74;
Short=PBP74;
AltName: Full=p66 MOT;
Flags: Precursor;
Name=Hspa9; Synonyms=Grp75, Hsp74, Hspa9a;
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].
STRAIN=CD-1-ICR; TISSUE=Embryonic fibroblast;
PubMed=8454632;
Wadhwa R., Kaul S.C., Ikawa Y., Sugimoto Y.;
"Identification of a novel member of mouse hsp70 family. Its
association with cellular mortal phenotype.";
J. Biol. Chem. 268:6615-6621(1993).
[2]
SEQUENCE REVISION TO 123.
Wadhwa R.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=CD-1-ICR; TISSUE=Embryonic fibroblast;
PubMed=7693662;
Wadhwa R., Kaul S.C., Sugimoto Y., Mitsui Y.;
"Induction of cellular senescence by transfection of cytosolic
mortalin cDNA in NIH 3T3 cells.";
J. Biol. Chem. 268:22239-22242(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=B-cell;
PubMed=7684501; DOI=10.1128/MCB.13.6.3598;
Domanico S.Z., Denagel D.C., Dahlseid J.N., Green J.M., Pierce S.K.;
"Cloning of the gene encoding peptide-binding protein 74 shows that it
is a new member of the heat shock protein 70 family.";
Mol. Cell. Biol. 13:3598-3610(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=8262211; DOI=10.1016/0014-5793(93)81602-V;
Michikawa Y., Baba T., Arai Y., Sakakura T., Kusakabe M.;
"Structure and organization of the gene encoding a mouse mitochondrial
stress-70 protein.";
FEBS Lett. 336:27-33(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeN; TISSUE=Kidney;
PubMed=7692847; DOI=10.1006/bbrc.1993.2238;
Michikawa Y., Baba T., Arai Y., Sakakura T., Tanaka M., Kusakabe M.;
"Antigenic protein specific for C3H strain mouse is a mitochondrial
stress-70 protein.";
Biochem. Biophys. Res. Commun. 196:223-232(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo, Kidney, and Liver;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; 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).
[11]
PROTEIN SEQUENCE OF 47-70.
TISSUE=Fibroblast;
PubMed=7523108; DOI=10.1002/elps.11501501101;
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
"Separation and sequencing of familiar and novel murine proteins using
preparative two-dimensional gel electrophoresis.";
Electrophoresis 15:735-745(1994).
[12]
PROTEIN SEQUENCE OF 188-202; 266-284; 349-360; 395-405 AND 499-513,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[13]
SUBCELLULAR LOCATION.
PubMed=7865888; DOI=10.1091/mbc.5.11.1265;
Dahlseid J.N., Lill R., Green J.M., Xu X., Qiu Y., Pierce S.K.;
"PBP74, a new member of the mammalian 70-kDa heat shock protein
family, is a mitochondrial protein.";
Mol. Biol. Cell 5:1265-1275(1994).
[14]
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).
[15]
FUNCTION.
PubMed=21123823; DOI=10.1182/blood-2010-06-293167;
Chen T.H., Kambal A., Krysiak K., Walshauser M.A., Raju G.,
Tibbitts J.F., Walter M.J.;
"Knockdown of Hspa9, a del(5q31.2) gene, results in a decrease in
hematopoietic progenitors in mice.";
Blood 117:1530-1539(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-300; LYS-360 AND
LYS-567, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-138;
LYS-206; LYS-300; LYS-360; LYS-368; LYS-394; LYS-567; LYS-600; LYS-610
AND LYS-646, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76; LYS-135; LYS-138;
LYS-206; LYS-234; LYS-288; LYS-300; LYS-360; LYS-567; LYS-600; LYS-612
AND LYS-646, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Chaperone protein which is implicated in the control of
cell proliferation and cellular aging. Plays a role in the
erythropoiesis process. {ECO:0000250|UniProtKB:P38646,
ECO:0000269|PubMed:21123823}.
-!- SUBUNIT: Interacts with FXN. Interacts with HSCB (By similarity).
Associates with the mitochondrial contact site and cristae
organizing system (MICOS) complex, composed of at least
MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60,
APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under
the names MINOS or MitOS complex. The MICOS complex associates
with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and
DNAJC11, mitochondrial inner membrane protein TMEM11 and with
HSPA9. Interacts with DNLZ, the interaction is required to prevent
self-aggregation (By similarity). Interacts with TESPA1 (By
similarity). Interacts with PDPN. {ECO:0000250|UniProtKB:P38646}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7865888}.
Nucleus, nucleolus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Found in all the cell types examined.
-!- INDUCTION: Not induced by heat shock, instead protein level is
decreased.
-!- POLYMORPHISM: Two forms of the protein have been found, MOT-1,
found in mortal cells and MOT-2, found in immortal cells. The
sequence of MOT-2 is shown here.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; D11089; BAA01862.2; -; mRNA.
EMBL; L06896; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; D17666; BAA04548.1; -; Genomic_DNA.
EMBL; D17556; BAA04493.1; -; mRNA.
EMBL; AK004946; BAB23690.1; -; mRNA.
EMBL; AK002634; BAB22248.1; -; mRNA.
EMBL; AK133501; BAE21690.1; -; mRNA.
EMBL; AK137109; BAE23238.1; -; mRNA.
EMBL; AK145965; BAE26790.1; -; mRNA.
EMBL; AK159791; BAE35373.1; -; mRNA.
EMBL; AK165958; BAE38486.1; -; mRNA.
EMBL; AK167856; BAE39874.1; -; mRNA.
EMBL; AC114820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466557; EDK97122.1; -; Genomic_DNA.
EMBL; BC052727; AAH52727.1; -; mRNA.
EMBL; BC057343; AAH57343.1; -; mRNA.
CCDS; CCDS29138.1; -.
PIR; S39839; A48127.
RefSeq; NP_034611.2; NM_010481.2.
UniGene; Mm.209419; -.
ProteinModelPortal; P38647; -.
SMR; P38647; -.
BioGrid; 200457; 20.
IntAct; P38647; 24.
MINT; MINT-1860030; -.
STRING; 10090.ENSMUSP00000025217; -.
iPTMnet; P38647; -.
PhosphoSitePlus; P38647; -.
SwissPalm; P38647; -.
COMPLUYEAST-2DPAGE; P38647; -.
REPRODUCTION-2DPAGE; IPI00133903; -.
REPRODUCTION-2DPAGE; P38647; -.
SWISS-2DPAGE; P38647; -.
EPD; P38647; -.
PaxDb; P38647; -.
PeptideAtlas; P38647; -.
PRIDE; P38647; -.
Ensembl; ENSMUST00000025217; ENSMUSP00000025217; ENSMUSG00000024359.
GeneID; 15526; -.
KEGG; mmu:15526; -.
UCSC; uc008elv.2; mouse.
CTD; 3313; -.
MGI; MGI:96245; Hspa9.
eggNOG; KOG0102; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00900000141262; -.
HOGENOM; HOG000228136; -.
HOVERGEN; HBG051845; -.
InParanoid; P38647; -.
KO; K04043; -.
OMA; ISIKRHM; -.
OrthoDB; EOG091G0386; -.
TreeFam; TF105046; -.
ChiTaRS; Hspa9; mouse.
PRO; PR:P38647; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024359; -.
CleanEx; MM_HSPA9; -.
Genevisible; P38647; MM.
GO; GO:0005737; C:cytoplasm; TAS:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IMP:UniProtKB.
GO; GO:1903707; P:negative regulation of hemopoiesis; IMP:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
GO; GO:0006457; P:protein folding; IEA:InterPro.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
HAMAP; MF_00332; DnaK; 1.
InterPro; IPR012725; Chaperone_DnaK.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
TIGRFAMs; TIGR02350; prok_dnaK; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Chaperone; Complete proteome;
Direct protein sequencing; Methylation; Mitochondrion;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transit peptide.
TRANSIT 1 46 Mitochondrion.
{ECO:0000269|PubMed:7523108}.
CHAIN 47 679 Stress-70 protein, mitochondrial.
/FTId=PRO_0000013564.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 87 87 Phosphothreonine.
{ECO:0000250|UniProtKB:P38646}.
MOD_RES 135 135 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 135 135 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 138 138 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 138 138 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 143 143 N6-acetyllysine.
{ECO:0000250|UniProtKB:P38646}.
MOD_RES 206 206 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 206 206 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 206 206 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 234 234 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 300 300 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 300 300 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 360 360 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 360 360 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 368 368 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 394 394 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:P38646}.
MOD_RES 513 513 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P38646}.
MOD_RES 567 567 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 567 567 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 600 600 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 600 600 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 610 610 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 612 612 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 646 646 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 646 646 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
VARIANT 618 618 M -> V (in MOT-1).
VARIANT 624 624 G -> R (in MOT-1).
CONFLICT 5 5 S -> T (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 78 78 L -> Q (in Ref. 7; BAE21690).
{ECO:0000305}.
CONFLICT 106 106 K -> R (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 150 150 G -> S (in Ref. 7; BAE35373).
{ECO:0000305}.
CONFLICT 522 522 F -> S (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 679 AA; 73461 MW; DF1C997775627928 CRC64;
MISASRAAAA RLVGTAASRS PAAARPQDGW NGLSHEAFRF VSRRDYASEA IKGAVVGIDL
GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT
KRLIGRRYDD PEVQKDTKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN
YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK
RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG
AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT
QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG
REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK
DQLPADECNK LKEEISKMRA LLAGKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE
GSGSSGTGEQ KEDQKEEKQ


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18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 96T
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.2 mg
10-782-55038 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
E0693h ELISA kit 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive pro 96T
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.1 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg


 

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