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

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DNAJB1P, 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, d ... show more
DNAJB1P, 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 show less
(194), (57), (54), (40), (34), (10), (9), (7), (4), (4), (4), (3), (3), (3), (3), (3), (3), (2), (2), (2), (1)
(151), (123)
Clonality (Clone)
Monoclonal ()
(12), (12), (8), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (1), (1), (1)
ELISA, Immunoprecipitation (IP), Western Blotting (WB)
(250), (128), (122), (122), (76), (65), (28), (20), (5), (5), (2)
Pubmed 7 references available
Quantity 100 μg
Shipping to United States ( )
Availability Will be delivered in 3 to 4 Business Days
Immunogen Full length protein yeast HSP40 (YDJ1)
Clone 1G10-H8
Specificity Detects ~40 kDa. Yeast specific product. Does not cross react with Human, Mouse or Rat.
Sensitivity 0.5 µg/mL of SMC-150 was sufficient for detection of 50 ng YDJ1 by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name HSP40 (DNAJB1 Antibody Abstract)
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). 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. (3, 4), 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 (7).
Cellular Localization: Cytoplasm | Nucleus
Gene ID 855661
NCBI Accession NP_014335
UniProt P25491
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:2000)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer 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
Supplier Images
Image no. 1 for anti-DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1) antibody (ABIN361660) SMC 150, Hsp40, YDJ1 (1G10 H8) 01.
Background publications 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).

Catalog No. ABIN361660
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