Hsp40 / Biotin / 1G10.H8

Product Details

Description	Mouse monoclonal to Hsp40, YDJ1 (Biotin). 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 . 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..
Conjugate	Biotin
Clone	1G10.H8
Target Species	Yeast
Applications	ELISA, WB, IP
Supplier	Biorbyt
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About Hsp40
This gene encodes a member of the DnaJ or Hsp40 (heat shock protein 40 kD) family of proteins. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. The encoded protein is a molecular chaperone that stimulates the ATPase activity of Hsp70 heat-shock proteins in order to promote protein folding and prevent misfolded protein aggregation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]

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