HSP40 Antibody

DnaJ (Hsp40) belongs to the DnaJ-class of molecular chaperones with a C-terminal Zn finger domain. HSP40 (DnaJ) together with DnaK and GrpE form a molecular chaperone that is involved in formation of protein complexes, protein folding, prevention of protein aggregation, and protein turnover and export. Several human neurodegenerative diseases involve the expansion of a polyglutamine within the disease proteins. Molecular chaperones such as HSP40 complexes can modulate polyglutamine pathogenesis In transgenic Drosophila disease models of Machado-Joseph disease and Huntington disease Hdj1, the Drosophila homolog to human HSP40, demonstrates substrate specificity for polyglutamine proteins suppression in combination with other molecular chapterones of neurotoxicity, and altered solubility of mutant polyglutamine proteins.

Store at 4˚ C for three months and -20˚ C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Ohtsuka, K., et al., Cell Stress Chaperones 5 (2) :98-112 (2000) . Hata, M., et al., Biochim. Biophys. Acta 1397 (1) :43-55 (1998) . Hata, M., et al., Genomics 38 (3) :446-449 (1996) . Ohtsuka, K., Biochem. Biophys. Res. Commun. 197 (1) :235-240 (1993) .

DnaJ homolog subfamily B member 1, DnaJ protein homolog 1, Heat shock 40 kDa protein 1, HSP40, Heat shock protein 40, Human DnaJ protein 1, hDj-1, DNAJB1, DNAJ1, HDJ1, HSPF1