HSP40, YDJ1 Antibody: ATTO 390

Category: Antibodies
Catalog
SMC-150D-A390
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Product Name HSP40, YDJ1 Antibody: ATTO 390
Description 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). Mouse Anti-Yeast HSP40, YDJ1 Monoclonal IgG1 Kappa
Synonyms DNAJA2 Antibody, CPR3 Antibody, HIRIP4 Antibody, DNAJ Antibody, DNJ3 Antibody, DJ3 Antibody, RDJ2 Antibody, HIRa interacting protein4 Antibody
Host Mouse
Clone 1G10.H8
Immunogen Full length protein yeast HSP40 (YDJ1)
Isotype IgG1 kappa
Specificity Detects ~40kDa. Yeast specific product. Does not cross react with Human, Mouse or Rat.
Reactivity Yeast
Applications ELISA, IP, WB
Form 50% glycerol, 0.09% sodium azide
Gene Id NP_014335.1. 855661
Uniprot P25491
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).
Supplier Stressmarq Biosciences

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