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

Details for Product No. ABIN361659, Supplier: Log in to see
Antigen
Reactivity
Yeast
187
61
58
41
34
9
8
8
5
4
4
3
3
3
3
3
2
2
2
2
1
Host
Mouse
154
114
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
13
13
9
7
7
7
7
7
7
7
7
7
7
7
7
7
7
1
1
Application
Immunoprecipitation (IP), ELISA, Western Blotting (WB)
239
124
123
118
77
63
20
19
4
4
2
Supplier
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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 for anti-DnaJ (Hsp40) Homolog, Subfamily B, Member 1 (DNAJB1) antibody (ABIN361659) 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).