HSP40, YDJ1 Antibody: Biotin

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).

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.

1. Cheetham M.E. and Caplan A.J. (1998) Cell Stress Chaperones 3: 28–36. 2. Fan C.Y., et al. (2003) Cell Stress Chaperones 8: 309–316. 3. Terda K., et al. (1997) J Cell Biol. 139: 1089-1095. 4. Lu Z. and Cyr D.M. (1998) J Biol Chem. 273: 27824-27830. 5. Liberek K. et al. (1991) Proc. Natl. Acad. Sci. USA 88: 2874–2878. 6. Cyr D.M., et al. (1992) J Biol Chem. 267: 20927–20931. 7. Höhfeld J., et al. (2001) EMBO Rep. 2: 885–890.