Hsp40/Hdj1 is a cytosolic co-chaperone belonging to the class DnaJ, named after its homolog in E. coli. Hsp40 functions in protein folding by binding nascent peptides and unfolded substrates and facilitating substrate interaction with Hsp70. Binding of Hsp40 to Hsp70 increases Hsp70 ATP hydrolysis and substrate binding, which is reversed by the action of nucleotide exchange factors (GrpE in E. coli). Repeated cycles of Hsp40/Hsp70 peptide binding and ATP hydrolysis prevent premature folding and aggregation, promoting protein maturation throughout the cell.
Regulatory Status:
RUO - Research Use Only
SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 2.0µg of purified Human HSP40 Protein (Prod. No .ADI-SPP-400).
Please mouse over
Product Literature References
Modulation of deregulated chaperone-mediated autophagy by a phosphopeptide: C. Macri, et al.; Autophagy 11, 472 (2015), Abstract; Full Text
Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineries: N.H. Benbahouche, et al.; J. Biol. Chem. 289, 6236 (2014), Application(s): Cell Culture, Abstract; Full Text
Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum: F. Ngansop, et al.; Biochem. Biophys. Res. Commun. 439, 191 (2013), Application(s): Luminescence Assay, Abstract;
Purification of hsp104, a protein disaggregase: E.A. Sweeny, et al.; J. Vis. Exp. 55, e3190 (2011), Application(s): Luminescence Assay, Abstract; Full Text
Antigen microarrays identify unique serum autoantibody signatures inclinical and pathologic subtypes of multiple sclerosis: H. Weiner, et al. ; PNAS 105, 18889 (2008), Application(s): Antigen Microarray , Abstract;
3'Sulfogalactolipid binding specifically inhibits HSP70 ATPase activity in vitro: C. Lingwood, et al. ; Biochemistry 42, 1611 (2003), Application(s): In Vitro Assay , Abstract;
Activation of the herpes simplex virus type-1 origin-binding protein (UL9) by heat shock proteins: P.E. Boehmer, et al. ; J. Biol. Chem. 277, 5660 (2002), Application(s): EMSA, In Vitro Assay , Abstract;
Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK: M.G. Katze, et al. ; PNAS 99, 15920 (2002), Application(s): In Vitro Assay , Abstract;
alpha-Crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner: A. Spector, et al. ; Eur. J. Biochem. 267, 4705 (2000), Application(s): In Vitro Assay , Abstract;
Ultra-sensitive (7 pg/ml) AMP'D® HSP70 high sensitivity ELISA kit enabling the ability to use less sample and detect both baseline and upregulated levels of human, mouse and rat Hsp70 (Hsp72), a major chaperone, cancer biomarker, and key cell stress regulator.
