|Calculated MW||H=38;M=38 KDa|
|Antigen Region||Full length|
|Other Names||DNAJB1; DNAJ1; HDJ1; HSPF1; DnaJ homolog subfamily B member 1; DnaJ protein homolog 1; Heat shock 40 kDa protein 1; Human DnaJ protein 1|
|Target/Specificity||This HSP40 antibody is generated from rabbits immunized with a recombinant protein encoding full length of human HSP40.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP40 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||DNAJ1, HDJ1, HSPF1|
|Function||Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877).|
|Cellular Location||Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Translocates rapidly from the cytoplasm to the nucleus, and especially to the nucleoli, upon heat shock|
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.
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).