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DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1) antibody

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  • HSP40
  • psiHSP40
  • CG10578
  • DNAJ-1
  • DNAJ1
  • DROJ1
  • Dmel\\CG10578
  • DnaJ1 64EF
  • DroJ1
  • EU3500
  • HSP40/HDJ1
  • Hdj1
  • Hsp-40
  • Hsp40
  • anon-WO0140519.166
  • anon-WO0172774.135
  • dHDJ1
  • dHDJ1/HSP40
  • dHdj1
  • dhdJ1
  • dhdj-1
  • dhdj1
  • dnaJ-1
  • droj1
  • hsp40
  • dnajb4
  • hdj1
  • hspf1
  • sis1
  • DnaJ-5
  • MAS5
  • dnaJ
  • HSPF1
  • RSPH16B
  • Sis1
  • 0610007I11Rik
Human, Mouse (Murine), Rat (Rattus)
Clonality (Clone)
Monoclonal ()
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
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Immunogen Recombinant Protein HSP40 (Hdj1)
Clone 3B9-E6
Specificity Detects ~40 kDa. Does not cross-react with HDJ2 or YDJ1.
Sensitivity 0.5 µg/mL of SMC-145 was sufficient for detection of Hsp40 (HDJ1) in 15 µg of HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Background Human HSP40/DnaJ proteins comprise a large protein family, members of which feature the J domain (named after the bacterial DnaJ protein) (1). The J-domain spans the first 75 N-terminal amino acids and is separated from the C-terminal by a glycine/phenylalanine-rich domain (2). Members of the HSP40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. In particular, Hdj1, the first human HSP40/DnaJ protein identified, plays an important role in protein translation and folding, as well as in the regulation of HSP70 function (3). HSP40 stimulates the ATPase activity of HSP70 which in turn causes conformational changes of the unfolded proteins (4, 5). The HSP40-HSP70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 which leads to protein folding, or components of protein degradation machinery CHIP and BAG-1 (6). Some studies have shown that the difference between HDJ1 and type 1 DNAJ proteins including HDJ2 and yeast YdjI is the result of the possession of a zinc finger domain by the latter, which helps in the function of protein folding. (7, 8).
Cellular Localization: Cytoplasm | Nucleus
Gene ID 3337
NCBI Accession NP_006136
UniProt P25685
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:2000), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Background publications Sohn, Kim, Kim et al.: "Negative regulation of hepatitis B virus replication by cellular Hsp40/DnaJ proteins through destabilization of viral core and X proteins." in: The Journal of general virology, Vol. 87, Issue Pt 7, pp. 1883-91, 2006 (PubMed).

Fan, Lee, Cyr: "Mechanisms for regulation of Hsp70 function by Hsp40." in: Cell stress & chaperones, Vol. 8, Issue 4, pp. 309-16, 2004 (PubMed).

Höhfeld, Cyr, Patterson: "From the cradle to the grave: molecular chaperones that may choose between folding and degradation." in: EMBO reports, Vol. 2, Issue 10, pp. 885-90, 2001 (PubMed).

Lu, Cyr: "Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1." in: The Journal of biological chemistry, Vol. 273, Issue 43, pp. 27824-30, 1998 (PubMed).

Cheetham, Caplan: "Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function." in: Cell stress & chaperones, Vol. 3, Issue 1, pp. 28-36, 1998 (PubMed).

Terada, Kanazawa, Bukau et al.: "The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding." in: The Journal of cell biology, Vol. 139, Issue 5, pp. 1089-95, 1997 (PubMed).

Liberek, Marszalek, Ang et al.: "Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 7, pp. 2874-8, 1991 (PubMed).

Cyr, Lu, Douglas: "Regulation of Hsp70 function by a eukaryotic DnaJ homolog." in: The Journal of biological chemistry, Vol. 267, Issue 29, pp. 20927-31, 1992 (PubMed).