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 (1G10-H8)

Host: Mouse

Reactivity: Yeast

Conjugate: Un-conjugated

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

Catalog no.: ABIN361659

Additional Information

Alternative name: Hsp40

Gene ID: 855661

UniProt: P25491

Immunogen: Full length protein yeast Hsp40 (YDJ1)

Cross-Reactivity (Details): Does not cross react with human, mouse or rat

Isotype: IgG1 kappa

Clone: 1G10-H8

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. There are two main types of Hsp40, type 1 DNAJ proteins including HDJ2 and yeast YdjI, type II includes yeast Sis1 and human Hdj1. Whereas type I possesses a zinc finger domain which helps in the function of protein folding., type II does not. Members of the Hsp40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. Hsp40 stimulates the ATPase activity of Hsp70 which in turn causes conformational changes of the unfolded proteins (5, 6). 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.

Synonyms: DNAJA2, CPR3, HIRIP4, DNAJ, DNJ3, DJ3, RDJ2, HIRa interatcting protein4

Characteristics: Accession Number: NP_014335.1

Specificity: Detects ~40kDa. Does not cross react with human, mouse, rat.

Sensitivity: 0.5 µg/mL of SMC-150 was sufficient for detection of 50ng YDJ1 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: 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

Images

SMC 150, Hsp40, YDJ1 (1G10 H8) 01.

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).