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

Antigen: DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1)

Synonyms: DNAJ1, DROJ1, DnaJ1 64EF, EU3500, HSP40, HSP40/HDJ1, Hsp-40, anon-WO0140519.166, anon-WO0172774.135, dHDJ1, dHDJ1/HSP40, dhdj-1, DmelCG10578, CG10578, psiHSP40, hdj1, sis1, hsp40, hspf1, dnajb4, MGC89364, Hsp40, DnaJ-5, MAS5, dnaJ

Clonality: Monoclonal (3B9-E6)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus)

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA

Catalog no.: ABIN361667

Additional Information

Alternative name: Hsp40

Gene ID: 3337

UniProt: P25685

Immunogen: Recombinant Protein Hsp40 (Hdj1)

Isotype: IgG1

Clone: 3B9-E6

Description: Human Hsp40/DnaJ proteins comprise a large protein family, members of which feature the J domain (named after the bacterial DnaJ protein). The J-domain spans the first 75 N-terminal amino acids and is separated from the C-terminal by a glycine/phenylalanine-rich domain. 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. HSP40 stimulates the ATPase activity of HSP70 which in turn causes conformational changes of the unfolded proteins. 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. 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..

Synonyms: DNAJ1, NDAJB1, HDJ1, Hsp40, HSPF1

Characteristics: Accession Number: NP_006136.1

Specificity: Detects ~40kDa. Does not cross-react with HDJ1 or YDJ1.

Sensitivity: 0.5 µg/mL of SMC-145 was sufficient for detection of Hsp40 (HDJ1) in 15µg of HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Synonyms: DNAJ1, DROJ1, DnaJ1 64EF, EU3500, HSP40, HSP40/HDJ1, Hsp-40, anon-WO0140519.166, anon-WO0172774.135, dHDJ1, dHDJ1/HSP40, dhdj-1, DmelCG10578, CG10578, psiHSP40, hdj1, sis1, hsp40, hspf1, dnajb4, MGC89364, Hsp40, DnaJ-5, MAS5, dnaJ

Application Details

Application Notes: 1:2000 (WB)

Concentration: 1mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.2, 50% glycerol

Storage: Store at -20° C. Shipping Conditions: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins, Signaling

Restrictions: For Research Use only

Publications

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).

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).

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).

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).

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).

Hoehfeld, 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).

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

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).