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DnaJ homolog subfamily B member 1 (DnaJ protein homolog 1) (Heat shock 40 kDa protein 1) (HSP40) (Heat shock protein 40) (Human DnaJ protein 1) (hDj-1)

 DNJB1_HUMAN             Reviewed;         340 AA.
P25685; B4DX52;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
18-JUL-2018, entry version 193.
RecName: Full=DnaJ homolog subfamily B member 1;
AltName: Full=DnaJ protein homolog 1;
AltName: Full=Heat shock 40 kDa protein 1;
Short=HSP40;
Short=Heat shock protein 40;
AltName: Full=Human DnaJ protein 1;
Short=hDj-1;
Name=DNAJB1; Synonyms=DNAJ1, HDJ1, HSPF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=1754405; DOI=10.1093/nar/19.23.6645;
Raabe T., Manley J.L.;
"A human homologue of the Escherichia coli DnaJ heat-shock protein.";
Nucleic Acids Res. 19:6645-6645(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 2-48.
TISSUE=Placenta;
PubMed=8250930; DOI=10.1006/bbrc.1993.2466;
Ohtsuka K.;
"Cloning of a cDNA for heat-shock protein hsp40, a human homologue of
bacterial DnaJ.";
Biochem. Biophys. Res. Commun. 197:235-240(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8975727; DOI=10.1006/geno.1996.0653;
Hata M., Okumura K., Seto M., Ohtsuka K.;
"Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1)
and its chromosomal localization to 19p13.2.";
Genomics 38:446-449(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Lung;
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).
[7]
PROTEIN SEQUENCE OF 2-49, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=1586970;
Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T.,
Tanabe K., Ohtsuka K.;
"Intracellular localization and partial amino acid sequence of a
stress-inducible 40-kDa protein in HeLa cells.";
Cell Struct. Funct. 17:77-86(1992).
[8]
FUNCTION, AND INTERACTION WITH HSF1.
PubMed=9499401; DOI=10.1101/gad.12.5.654;
Shi Y., Mosser D.D., Morimoto R.I.;
"Molecular chaperones as HSF1-specific transcriptional repressors.";
Genes Dev. 12:654-666(1998).
[9]
INTERACTION WITH DNAJC3.
PubMed=9920933; DOI=10.1074/jbc.274.6.3797;
Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I.,
Katze M.G.;
"The cellular inhibitor of the PKR protein kinase, P58(IPK), is an
influenza virus-activated co-chaperone that modulates heat shock
protein 70 activity.";
J. Biol. Chem. 274:3797-3803(1999).
[10]
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, 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).
[13]
FUNCTION.
PubMed=24318877; DOI=10.1074/jbc.M113.521997;
Rauch J.N., Gestwicki J.E.;
"Binding of human nucleotide exchange factors to heat shock protein 70
(Hsp70) generates functionally distinct complexes in vitro.";
J. Biol. Chem. 289:1402-1414(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
STRUCTURE BY NMR OF 1-76.
PubMed=8764402; DOI=10.1006/jmbi.1996.0394;
Qian Y.Q., Patel D., Hartl F.-U., McColl D.J.;
"Nuclear magnetic resonance solution structure of the human Hsp40
(HDJ-1) J-domain.";
J. Mol. Biol. 260:224-235(1996).
-!- FUNCTION: Interacts with HSP70 and can stimulate its ATPase
activity. Stimulates the association between HSC70 and HIP.
Negatively regulates heat shock-induced HSF1 transcriptional
activity during the attenuation and recovery phase period of the
heat shock response (PubMed:9499401). Stimulates ATP hydrolysis
and the folding of unfolded proteins mediated by HSPA1A/B (in
vitro) (PubMed:24318877). {ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:9499401}.
-!- SUBUNIT: Interacts with DNAJC3 (PubMed:9920933). Interacts with
HSF1 (via transactivation domain); this interaction results in the
inhibition of heat shock- and HSF1-induced transcriptional
activity during the attenuation and recovery phase period of the
heat shock response (PubMed:9499401). {ECO:0000269|PubMed:9499401,
ECO:0000269|PubMed:9920933}.
-!- INTERACTION:
Q9Y266:NUDC; NbExp=3; IntAct=EBI-357034, EBI-357298;
Q62392:Phlda1 (xeno); NbExp=2; IntAct=EBI-357034, EBI-309727;
P54274:TERF1; NbExp=2; IntAct=EBI-357034, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1586970}.
Nucleus {ECO:0000269|PubMed:1586970}. Nucleus, nucleolus
{ECO:0000269|PubMed:1586970}. Note=Translocates rapidly from the
cytoplasm to the nucleus, and especially to the nucleoli, upon
heat shock.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P25685-1; Sequence=Displayed;
Name=2;
IsoId=P25685-2; Sequence=VSP_056414;
Note=No experimental confirmation available.;
-!- INDUCTION: By heat shock. {ECO:0000269|PubMed:1586970}.
-!- SEQUENCE CAUTION:
Sequence=CAA44287.1; Type=Frameshift; Positions=11, 28, 81, 136; Evidence={ECO:0000305};
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EMBL; X62421; CAA44287.1; ALT_FRAME; mRNA.
EMBL; D49547; BAA08495.1; -; mRNA.
EMBL; D85429; BAA12819.1; -; Genomic_DNA.
EMBL; AK301817; BAG63264.1; -; mRNA.
EMBL; AC009004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC012318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002352; AAH02352.1; -; mRNA.
EMBL; BC019827; AAH19827.1; -; mRNA.
CCDS; CCDS12312.1; -. [P25685-1]
CCDS; CCDS74295.1; -. [P25685-2]
PIR; JN0912; JN0912.
PIR; S20062; S20062.
RefSeq; NP_001287843.1; NM_001300914.1. [P25685-2]
RefSeq; NP_001300893.1; NM_001313964.1. [P25685-2]
RefSeq; NP_006136.1; NM_006145.2. [P25685-1]
RefSeq; XP_006722796.1; XM_006722733.1. [P25685-2]
RefSeq; XP_006722797.1; XM_006722734.3. [P25685-2]
RefSeq; XP_011526258.1; XM_011527956.2. [P25685-2]
UniGene; Hs.515210; -.
PDB; 1HDJ; NMR; -; A=1-76.
PDB; 2QLD; X-ray; 2.70 A; A=158-340.
PDB; 3AGX; X-ray; 1.85 A; A/B=161-340.
PDB; 3AGY; X-ray; 1.85 A; A/B=161-340.
PDB; 3AGZ; X-ray; 2.51 A; A/B=151-340.
PDB; 4WB7; X-ray; 1.90 A; A/B=2-70.
PDBsum; 1HDJ; -.
PDBsum; 2QLD; -.
PDBsum; 3AGX; -.
PDBsum; 3AGY; -.
PDBsum; 3AGZ; -.
PDBsum; 4WB7; -.
ProteinModelPortal; P25685; -.
SMR; P25685; -.
BioGrid; 109569; 108.
CORUM; P25685; -.
DIP; DIP-41180N; -.
IntAct; P25685; 54.
MINT; P25685; -.
STRING; 9606.ENSP00000254322; -.
iPTMnet; P25685; -.
PhosphoSitePlus; P25685; -.
BioMuta; DNAJB1; -.
DMDM; 1706473; -.
REPRODUCTION-2DPAGE; IPI00015947; -.
EPD; P25685; -.
PaxDb; P25685; -.
PeptideAtlas; P25685; -.
PRIDE; P25685; -.
ProteomicsDB; 54280; -.
DNASU; 3337; -.
Ensembl; ENST00000254322; ENSP00000254322; ENSG00000132002. [P25685-1]
Ensembl; ENST00000396969; ENSP00000444212; ENSG00000132002. [P25685-2]
GeneID; 3337; -.
KEGG; hsa:3337; -.
UCSC; uc010xnr.2; human. [P25685-1]
CTD; 3337; -.
DisGeNET; 3337; -.
EuPathDB; HostDB:ENSG00000132002.7; -.
GeneCards; DNAJB1; -.
H-InvDB; HIX0014838; -.
HGNC; HGNC:5270; DNAJB1.
HPA; CAB017450; -.
HPA; HPA063247; -.
MalaCards; DNAJB1; -.
MIM; 604572; gene.
neXtProt; NX_P25685; -.
OpenTargets; ENSG00000132002; -.
Orphanet; 401920; Fibrolamellar hepatocellular carcinoma.
PharmGKB; PA27412; -.
eggNOG; KOG0714; Eukaryota.
eggNOG; COG0484; LUCA.
GeneTree; ENSGT00760000118947; -.
HOGENOM; HOG000226718; -.
HOVERGEN; HBG066727; -.
InParanoid; P25685; -.
KO; K09507; -.
OMA; GAYTYQF; -.
OrthoDB; EOG091G0DLS; -.
PhylomeDB; P25685; -.
TreeFam; TF105141; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-3371568; Attenuation phase.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
SIGNOR; P25685; -.
ChiTaRS; DNAJB1; human.
EvolutionaryTrace; P25685; -.
GeneWiki; DNAJB1; -.
GenomeRNAi; 3337; -.
PRO; PR:P25685; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000132002; -.
CleanEx; HS_DNAJB1; -.
ExpressionAtlas; P25685; baseline and differential.
Genevisible; P25685; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0061827; C:sperm head; IEA:Ensembl.
GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IDA:UniProtKB.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:BHF-UCL.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR036869; J_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 2.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chaperone; Complete proteome;
Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome; Stress response.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1586970,
ECO:0000269|PubMed:8250930}.
CHAIN 2 340 DnaJ homolog subfamily B member 1.
/FTId=PRO_0000071016.
DOMAIN 2 70 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
MOD_RES 307 307 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 100 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056414.
CONFLICT 68 68 G -> L (in Ref. 1; CAA44287).
{ECO:0000305}.
CONFLICT 150 150 R -> C (in Ref. 1; CAA44287).
{ECO:0000305}.
CONFLICT 183 183 M -> T (in Ref. 1; CAA44287).
{ECO:0000305}.
CONFLICT 320 320 V -> A (in Ref. 1; CAA44287).
{ECO:0000305}.
HELIX 5 9 {ECO:0000244|PDB:4WB7}.
HELIX 17 31 {ECO:0000244|PDB:4WB7}.
TURN 33 35 {ECO:0000244|PDB:4WB7}.
HELIX 41 55 {ECO:0000244|PDB:4WB7}.
HELIX 58 70 {ECO:0000244|PDB:4WB7}.
STRAND 166 170 {ECO:0000244|PDB:3AGX}.
HELIX 172 177 {ECO:0000244|PDB:3AGX}.
STRAND 179 190 {ECO:0000244|PDB:3AGX}.
TURN 191 193 {ECO:0000244|PDB:2QLD}.
STRAND 197 208 {ECO:0000244|PDB:3AGX}.
STRAND 217 220 {ECO:0000244|PDB:3AGX}.
STRAND 228 230 {ECO:0000244|PDB:3AGX}.
STRAND 235 241 {ECO:0000244|PDB:3AGX}.
STRAND 248 250 {ECO:0000244|PDB:3AGX}.
STRAND 253 261 {ECO:0000244|PDB:3AGX}.
HELIX 262 267 {ECO:0000244|PDB:3AGX}.
STRAND 269 274 {ECO:0000244|PDB:3AGX}.
STRAND 280 285 {ECO:0000244|PDB:3AGX}.
STRAND 294 297 {ECO:0000244|PDB:3AGX}.
STRAND 305 307 {ECO:0000244|PDB:3AGX}.
STRAND 314 321 {ECO:0000244|PDB:3AGX}.
HELIX 328 337 {ECO:0000244|PDB:3AGX}.
SEQUENCE 340 AA; 38044 MW; 17545098B0C196DF CRC64;
MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK
REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA MFAEFFGGRN PFDTFFGQRN
GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT
KKMKISHKRL NPDGKSIRNE DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK
DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE
GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI


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10-782-55040 DnaJ homolog subfamily B member 1 - Heat shock 40 kDa protein 1; Heat shock protein 40; HSP40; DnaJ protein homolog 1; HDJ-1 N_A 0.2 mg
10-782-55040 DnaJ homolog subfamily B member 1 - Heat shock 40 kDa protein 1; Heat shock protein 40; HSP40; DnaJ protein homolog 1; HDJ-1 N_A 0.05 mg
EIAAB11548 DnaJ homolog subfamily B member 5,DNAJB5,Heat shock protein cognate 40,Heat shock protein Hsp40-2,Heat shock protein Hsp40-3,Homo sapiens,Hsc40,HSC40,Human
E0872m ELISA DnaJ homolog subfamily B member 1,Dnajb1,Heat shock 40 kDa protein 1,Heat shock protein 40,HSP40,Hsp40,Hspf1,Mouse,Mus musculus 96T
U0872m CLIA DnaJ homolog subfamily B member 1,Dnajb1,Heat shock 40 kDa protein 1,Heat shock protein 40,HSP40,Hsp40,Hspf1,Mouse,Mus musculus 96T
E0872m ELISA kit DnaJ homolog subfamily B member 1,Dnajb1,Heat shock 40 kDa protein 1,Heat shock protein 40,HSP40,Hsp40,Hspf1,Mouse,Mus musculus 96T
18-003-42920 DnaJ homolog subfamily B member 5 - Heat shock protein Hsp40-3; Heat shock protein cognate 40; Hsc40; Hsp40-2 Polyclonal 0.1 mg Protein A
EIAAB11543 DnaJ homolog subfamily B member 3,DnaJ protein homolog 3,Dnajb3,Heat shock protein J3,Hsj3,HSJ-3,Mouse,Msj1,MSJ-1,Mus musculus
EIAAB11532 DnaJ homolog subfamily A member 1,Dnaja1,DnaJ-like protein 1,Heat shock protein J2,Hsj2,HSJ-2,Rat,Rattus norvegicus,Rdj1
EIAAB11300 ABBP-2,APOBEC1-binding protein 2,DnaJ homolog subfamily B member 11,DnaJ protein homolog 9,DNAJB11,EDJ,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERJ3,ERj3p
EIAAB11549 DnaJ homolog subfamily B member 5,Dnajb5,Heat shock protein cognate 40,Heat shock protein Hsp40-3,Hsc40,Hsc40,Mouse,Mus musculus
EIAAB11554 DnaJ homolog subfamily B member 6,Dnajb6,Heat shock protein J2,HSJ-2,Hsp40 homolog,MRJ,MSJ-1,Rat,Rattus norvegicus
EIAAB11298 ABBP-2,APOBEC1-binding protein 2,DnaJ homolog subfamily B member 11,Dnajb11,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p,Mouse,Mus musculus
EIAAB11297 DnaJ homolog subfamily B member 11,Dnajb11,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p,Liver regeneration-related protein LRRGT00084,Rat,Rattus norvegi
EIAAB11301 Bos taurus,Bovine,DnaJ homolog subfamily B member 11,DNAJB11,ER-associated DNAJ,ER-associated dnaJ protein 3,ER-associated Hsp40 co-chaperone,ERdj3,ERj3p
hsp-050 Recombinant Human DnaJ (Hsp40) Homolog Subfamily B Member 8 HEAT SHOCK PROTEINS 25
hsp-035 Recombinant Human DnaJ (Hsp40) Homolog Subfamily B Member 2 HEAT SHOCK PROTEINS 10
hsp-038 Recombinant Human DnaJ (Hsp40) Homolog Subfamily B Member 6 HEAT SHOCK PROTEINS 5


 

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