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Chaperone protein DnaJ (HSP40) (Heat shock protein J)

 DNAJ_ECOLI              Reviewed;         376 AA.
P08622;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 188.
RecName: Full=Chaperone protein DnaJ;
AltName: Full=HSP40;
AltName: Full=Heat shock protein J;
Name=dnaJ; Synonyms=groP; OrderedLocusNames=b0015, JW0014;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6.
PubMed=3003084;
Ohki M., Tamura F., Nishimura S., Uchida H.;
"Nucleotide sequence of the Escherichia coli dnaJ gene and
purification of the gene product.";
J. Biol. Chem. 261:1778-1781(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3003085;
Bardwell J.C.A., Tilly K., Craig E., King J., Zylicz M.,
Georgopoulos C.;
"The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A
gene that encodes a heat shock protein.";
J. Biol. Chem. 261:1782-1785(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
PubMed=1630901; DOI=10.1093/nar/20.13.3305;
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION.
PubMed=1826368; DOI=10.1073/pnas.88.7.2874;
Liberek K., Marszalek J., Ang D., Georgopoulos C., Zylicz M.;
"Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate
ATPase activity of DnaK.";
Proc. Natl. Acad. Sci. U.S.A. 88:2874-2878(1991).
[7]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[8]
FUNCTION.
PubMed=15302880; DOI=10.1074/jbc.M402405200;
Zietkiewicz S., Krzewska J., Liberek K.;
"Successive and synergistic action of the Hsp70 and Hsp100 chaperones
in protein disaggregation.";
J. Biol. Chem. 279:44376-44383(2004).
[9]
ROLE IN HEAT-SHOCK RESPONSE.
PubMed=15044009; DOI=10.1016/S0014-5793(04)00190-5;
Siegenthaler R.K., Grimshaw J.P., Christen P.;
"Immediate response of the DnaK molecular chaperone system to heat
shock.";
FEBS Lett. 562:105-110(2004).
[10]
DISRUPTION PHENOTYPE.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
PubMed=14726952; DOI=10.1038/sj.embor.7400067;
Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S.,
Hartl F.U., Georgopoulos C.;
"In vivo analysis of the overlapping functions of DnaK and trigger
factor.";
EMBO Rep. 5:195-200(2004).
[11]
INTERACTION WITH DNAK.
PubMed=14729677; DOI=10.1074/jbc.M308782200;
Watanabe Y.H., Yoshida M.;
"Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress
converts the former to the latter, and only the latter can do
disaggregation in cooperation with ClpB.";
J. Biol. Chem. 279:15723-15727(2004).
[12]
ROLE IN PLASMID DNA REPLICATION.
PubMed=15485812; DOI=10.1074/jbc.M407531200;
Zzaman S., Reddy J.M., Bastia D.;
"The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi
initiator protein of R6K into a form active in replication
initiation.";
J. Biol. Chem. 279:50886-50894(2004).
[13]
MUTAGENESIS OF HIS-33.
PubMed=8106526;
Wall D., Zylicz M., Georgopoulos C.;
"The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein
stimulate the ATPase activity of DnaK and are sufficient for lambda
replication.";
J. Biol. Chem. 269:5446-5451(1994).
[14]
MUTAGENESIS OF ASP-35.
PubMed=9860950; DOI=10.1073/pnas.95.26.15223;
Suh W.-C., Burkholder W.F., Lu C.Z., Zhao X., Gottesman M.E.,
Gross C.A.;
"Interaction of the Hsp70 molecular chaperone, DnaK, with its
cochaperone DnaJ.";
Proc. Natl. Acad. Sci. U.S.A. 95:15223-15228(1998).
[15]
MUTAGENESIS OF ARG-19; GLU-20; 25-TYR--GLN-38; LYS-41; GLU-42; GLU-44;
46-LYS--GLU-49; LYS-51; GLU-52; TYR-54; GLU-55; 58-THR--ARG-63; ASP-67
AND GLN-68.
PubMed=12454054;
Genevaux P., Schwager F., Georgopoulos C., Kelley W.L.;
"Scanning mutagenesis identifies amino acid residues essential for the
in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.";
Genetics 162:1045-1053(2002).
[16]
MUTAGENESIS OF CYS-144; CYS-147; CYS-161; CYS-164; CYS-183; CYS-186;
CYS-197 AND CYS-200.
PubMed=12941935; DOI=10.1074/jbc.M307491200;
Linke K., Wolfram T., Bussemer J., Jakob U.;
"The roles of the two zinc binding sites in DnaJ.";
J. Biol. Chem. 278:44457-44466(2003).
[17]
MUTAGENESIS OF CYS-161; CYS-164; CYS-183 AND CYS-186.
PubMed=15683252; DOI=10.1021/bi0480943;
Shi Y.-Y., Tang W., Hao S.-F., Wang C.-C.;
"Contributions of cysteine residues in Zn2 to zinc fingers and thiol-
disulfide oxidoreductase activities of chaperone DnaJ.";
Biochemistry 44:1683-1689(2005).
[18]
STRUCTURE BY NMR OF 1-108.
PubMed=8764403; DOI=10.1006/jmbi.1996.0395;
Pellechia M., Szyperski T., Wall D., Georgopoulos C., Wuethrich K.;
"NMR structure of the J-domain and the Gly/Phe-rich region of the
Escherichia coli DnaJ chaperone.";
J. Mol. Biol. 260:236-250(1996).
[19]
STRUCTURE BY NMR OF 1-105.
PubMed=10210198; DOI=10.1110/ps.8.1.203;
Huang K., Flanagan J.M., Prestegard J.H.;
"The influence of C-terminal extension on the structure of the 'J-
domain' in E. coli DnaJ.";
Protein Sci. 8:203-214(1999).
[20]
STRUCTURE BY NMR OF 131-209.
PubMed=10891270; DOI=10.1006/jmbi.2000.3923;
Martinez-Yamout M., Legge G.B., Zhang O., Wright P.E., Dyson H.J.;
"Solution structure of the cysteine-rich domain of the Escherichia
coli chaperone protein DnaJ.";
J. Mol. Biol. 300:805-818(2000).
-!- FUNCTION: Interacts with DnaK and GrpE to disassemble a protein
complex at the origins of replication of phage lambda and several
plasmids. Participates actively in the response to hyperosmotic
and heat shock by preventing the aggregation of stress-denatured
proteins and by disaggregating proteins, also in an autonomous,
DnaK-independent fashion. Unfolded proteins bind initially to
DnaJ; upon interaction with the DnaJ-bound protein, DnaK
hydrolyzes its bound ATP, resulting in the formation of a stable
complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers
the release of the substrate protein, thus completing the reaction
cycle. Several rounds of ATP-dependent interactions between DnaJ,
DnaK and GrpE are required for fully efficient folding.
{ECO:0000269|PubMed:15044009, ECO:0000269|PubMed:15302880,
ECO:0000269|PubMed:15485812, ECO:0000269|PubMed:1826368}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per monomer.;
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P0A6Y8:dnaK; NbExp=8; IntAct=EBI-545285, EBI-542092;
P06993:malT; NbExp=5; IntAct=EBI-545285, EBI-542934;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- INDUCTION: By heat shock under the control of the HtpR regulatory
protein.
-!- DOMAIN: The J domain is necessary and sufficient to stimulate DnaK
ATPase activity. Zinc center 1 plays an important role in the
autonomous, DnaK-independent chaperone activity of DnaJ. Zinc
center 2 is essential for interaction with DnaK and for DnaJ
activity.
-!- DISRUPTION PHENOTYPE: Single dnaJ and double dnaK-dnaJ disruption
are non-essential; synthetic lethality is seen in a triple tig-
dnaK-dnaJ disruption, although this depends on temperature (triple
disruptions grow slowly at 20 and 34 degrees Celsius but not at 43
degrees) and strain background. {ECO:0000269|PubMed:14726952}.
-!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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EMBL; M12544; AAA00009.1; -; Genomic_DNA.
EMBL; M12565; AAA23693.1; -; Genomic_DNA.
EMBL; U00096; AAC73126.1; -; Genomic_DNA.
EMBL; AP009048; BAB96590.1; -; Genomic_DNA.
PIR; A92572; HHECDJ.
RefSeq; NP_414556.1; NC_000913.3.
RefSeq; WP_001118476.1; NZ_LN832404.1.
PDB; 1BQ0; NMR; -; A=2-104.
PDB; 1BQZ; NMR; -; A=2-78.
PDB; 1EXK; NMR; -; A=131-209.
PDB; 1XBL; NMR; -; A=2-108.
PDBsum; 1BQ0; -.
PDBsum; 1BQZ; -.
PDBsum; 1EXK; -.
PDBsum; 1XBL; -.
ProteinModelPortal; P08622; -.
SMR; P08622; -.
BioGrid; 4259725; 242.
BioGrid; 849156; 1.
DIP; DIP-9460N; -.
IntAct; P08622; 101.
MINT; MINT-1220303; -.
STRING; 316385.ECDH10B_0015; -.
PaxDb; P08622; -.
PRIDE; P08622; -.
EnsemblBacteria; AAC73126; AAC73126; b0015.
EnsemblBacteria; BAB96590; BAB96590; BAB96590.
GeneID; 944753; -.
KEGG; ecj:JW0014; -.
KEGG; eco:b0015; -.
PATRIC; fig|1411691.4.peg.2269; -.
EchoBASE; EB0236; -.
EcoGene; EG10240; dnaJ.
eggNOG; ENOG4105BZ5; Bacteria.
eggNOG; COG0484; LUCA.
HOGENOM; HOG000226717; -.
InParanoid; P08622; -.
KO; K03686; -.
PhylomeDB; P08622; -.
BioCyc; EcoCyc:EG10240-MONOMER; -.
BioCyc; MetaCyc:EG10240-MONOMER; -.
EvolutionaryTrace; P08622; -.
PRO; PR:P08622; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:EcoliWiki.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0051087; F:chaperone binding; IPI:CAFA.
GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
GO; GO:0003756; F:protein disulfide isomerase activity; IDA:EcoliWiki.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:EcoCyc.
GO; GO:0016989; F:sigma factor antagonist activity; IDA:EcoCyc.
GO; GO:0051082; F:unfolded protein binding; IDA:CAFA.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:EcoCyc.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:CAFA.
GO; GO:0006260; P:DNA replication; IMP:EcoliWiki.
GO; GO:0006461; P:protein complex assembly; IDA:CAFA.
GO; GO:0006457; P:protein folding; IDA:EcoliWiki.
GO; GO:0042026; P:protein refolding; IDA:EcoliWiki.
GO; GO:0009408; P:response to heat; IMP:EcoCyc.
GO; GO:0016032; P:viral process; IDA:EcoCyc.
CDD; cd06257; DnaJ; 1.
CDD; cd10719; DnaJ_zf; 1.
Gene3D; 1.10.287.110; -; 1.
HAMAP; MF_01152; DnaJ; 1.
InterPro; IPR012724; DnaJ.
InterPro; IPR002939; DnaJ_C.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR008971; HSP40/DnaJ_pept-bd.
InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF01556; DnaJ_C; 1.
Pfam; PF00684; DnaJ_CXXCXGXG; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF49493; SSF49493; 3.
SUPFAM; SSF57938; SSF57938; 1.
TIGRFAMs; TIGR02349; DnaJ_bact; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51188; ZF_CR; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA replication; Metal-binding;
Reference proteome; Repeat; Stress response; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3003084}.
CHAIN 2 376 Chaperone protein DnaJ.
/FTId=PRO_0000070777.
DOMAIN 3 72 J.
REPEAT 144 151 CXXCXGXG motif.
REPEAT 161 168 CXXCXGXG motif.
REPEAT 183 190 CXXCXGXG motif.
REPEAT 197 204 CXXCXGXG motif.
ZN_FING 131 209 CR-type.
COMPBIAS 77 114 Gly-rich.
METAL 144 144 Zinc 1.
METAL 147 147 Zinc 1.
METAL 161 161 Zinc 2.
METAL 164 164 Zinc 2.
METAL 183 183 Zinc 2.
METAL 186 186 Zinc 2.
METAL 197 197 Zinc 1.
METAL 200 200 Zinc 1.
MUTAGEN 19 20 RE->AA: No effect.
MUTAGEN 25 25 Y->A: Loss of activity.
MUTAGEN 26 26 K->A: Loss of activity.
MUTAGEN 27 27 R->A: No effect.
MUTAGEN 28 28 L->A: No effect.
MUTAGEN 29 29 A->G: No effect.
MUTAGEN 30 31 MK->AA: No effect.
MUTAGEN 32 32 Y->A: No effect.
MUTAGEN 33 33 H->Q: Loss of ability to stimulate DnaK
ATPase activity.
{ECO:0000269|PubMed:8106526}.
MUTAGEN 34 34 P->F: Loss of function.
MUTAGEN 35 35 D->N: Loss of ability to bind DnaK.
{ECO:0000269|PubMed:9860950}.
MUTAGEN 36 36 R->A: Decrease in chaperone function.
MUTAGEN 37 37 N->A: Decrease in chaperone function.
MUTAGEN 38 38 Q->A: No effect.
MUTAGEN 41 42 KE->AA: No effect.
MUTAGEN 44 44 E->A: No effect.
{ECO:0000269|PubMed:12454054}.
MUTAGEN 46 46 K->A: No effect.
MUTAGEN 47 47 F->A: Loss of function.
MUTAGEN 48 49 KE->AA: No effect.
MUTAGEN 51 52 KE->AA: No effect.
MUTAGEN 54 54 Y->A: No effect.
{ECO:0000269|PubMed:12454054}.
MUTAGEN 55 55 E->A: No effect.
{ECO:0000269|PubMed:12454054}.
MUTAGEN 58 59 TD->AA: No effect.
MUTAGEN 60 61 SQ->AA: No effect.
MUTAGEN 62 63 KR->AA: No effect.
MUTAGEN 67 68 DQ->AA: No effect.
MUTAGEN 144 144 C->S: Loss of DnaK-independent chaperone
activity; when associated with S-147; S-
197 and S-200.
{ECO:0000269|PubMed:12941935}.
MUTAGEN 147 147 C->S: Loss of DnaK-independent chaperone
activity; when associated with S-144; S-
197 and S-200.
{ECO:0000269|PubMed:12941935}.
MUTAGEN 161 161 C->H: No effect on chaperone function;
when associated with H-183.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 161 161 C->S: Loss of function; when associated
with S-164; S-183 and S-186.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 164 164 C->H: No effect on chaperone function;
when associated with H-183.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 164 164 C->S: Loss of function; when associated
with S-161; S-183 and S-186.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 183 183 C->H: No effect on chaperone function.
Same effect; when associated with H-161
or H-164. {ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 183 183 C->S: Loss of function; when associated
with S-161; S-164 and S-186.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 186 186 C->H: No effect on chaperone function.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 186 186 C->S: Loss of function; when associated
with S-161; S-164 and S-184.
{ECO:0000269|PubMed:12941935,
ECO:0000269|PubMed:15683252}.
MUTAGEN 197 197 C->S: Loss of DnaK-independent chaperone
activity; when associated with S-144; S-
147 and S-200.
{ECO:0000269|PubMed:12941935}.
MUTAGEN 200 200 C->S: Loss of DnaK-independent chaperone
activity; when associated with S-144; S-
147 and S-197.
{ECO:0000269|PubMed:12941935}.
TURN 7 10 {ECO:0000244|PDB:1BQ0}.
STRAND 13 15 {ECO:0000244|PDB:1XBL}.
HELIX 18 29 {ECO:0000244|PDB:1BQ0}.
TURN 30 32 {ECO:0000244|PDB:1BQ0}.
TURN 34 36 {ECO:0000244|PDB:1BQ0}.
TURN 38 40 {ECO:0000244|PDB:1BQ0}.
HELIX 43 50 {ECO:0000244|PDB:1BQ0}.
TURN 51 55 {ECO:0000244|PDB:1BQ0}.
HELIX 61 65 {ECO:0000244|PDB:1BQ0}.
TURN 66 68 {ECO:0000244|PDB:1BQ0}.
TURN 70 72 {ECO:0000244|PDB:1BQ0}.
TURN 132 134 {ECO:0000244|PDB:1EXK}.
STRAND 141 143 {ECO:0000244|PDB:1EXK}.
HELIX 145 147 {ECO:0000244|PDB:1EXK}.
TURN 148 150 {ECO:0000244|PDB:1EXK}.
STRAND 154 156 {ECO:0000244|PDB:1EXK}.
TURN 162 166 {ECO:0000244|PDB:1EXK}.
STRAND 167 174 {ECO:0000244|PDB:1EXK}.
STRAND 177 182 {ECO:0000244|PDB:1EXK}.
TURN 184 188 {ECO:0000244|PDB:1EXK}.
STRAND 189 192 {ECO:0000244|PDB:1EXK}.
STRAND 194 196 {ECO:0000244|PDB:1EXK}.
HELIX 198 200 {ECO:0000244|PDB:1EXK}.
STRAND 203 207 {ECO:0000244|PDB:1EXK}.
SEQUENCE 376 AA; 41100 MW; 05FA762EF9844532 CRC64;
MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI KEAYEVLTDS
QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD IFGGGRGRQR AARGADLRYN
MELTLEEAVR GVTKEIRIPT LEECDVCHGS GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ
QTCPHCQGRG TLIKDPCNKC HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP
AGDLYVQVQV KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG
KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG PTGEHNSPRS
KSFFDGVKKF FDDLTR


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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
DnaJ-317E Protein: Recombinant E.coli DnaJ Chaperone Hsp40, Co-chaperone with DnaK (1-376) 20ug
DnaJ-317E Protein Recombinant E.coli DnaJ Chaperone Hsp40, Co-chaperone with DnaK (1-376) 20ug
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
EIAAB11531 DnaJ homolog subfamily A member 1,DnaJ protein homolog 2,DNAJ2,DNAJA1,HDJ2,hDj-2,Heat shock 40 kDa protein 4,Heat shock protein J2,Homo sapiens,HSDJ,HSJ2,HSJ-2,HSPF4,Human,Human DnaJ protein 2
228-10327-1 Recombinant Heat Shock Protein 40 (HSP40) _ DnaJ 20
228-10327-2 Recombinant Heat Shock Protein 40 (HSP40) _ DnaJ 100
228-10327-3 Recombinant Heat Shock Protein 40 (HSP40) _ DnaJ 1 mg
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
228-10328-2 Recombinant Human Heat Shock Protein 40 (HSP40) _ DnaJ 25
228-10328-3 Recombinant Human Heat Shock Protein 40 (HSP40) _ DnaJ 1 mg
228-10328-1 Recombinant Human Heat Shock Protein 40 (HSP40) _ DnaJ 5


 

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