|Reactivity||Human, Mouse, Rat|
|Calculated MW||10 KDa|
|Other Names||10 kDa heat shock protein, mitochondrial, Hsp10, 10 kDa chaperonin, Chaperonin 10, CPN10, Early-pregnancy factor, EPF, HSPE1|
|Target/Specificity||KLH conjugated synthetic peptide derived from human HSPE1|
|Format||0.01M PBS, pH 7.2, 0.1% Sodium azide, Glycerol 50%|
|Storage||Store at -20 °C.Stable for 12 months from date of receipt|
|Function||Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:7912672, PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).|
|Cellular Location||Mitochondrion matrix.|
Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
Monzini N.,et al.Biochim. Biophys. Acta 1218:478-480(1994).
Chen J.J.,et al.Biochim. Biophys. Acta 1219:189-190(1994).
Hansen J.J.,et al.Hum. Genet. 112:71-77(2003).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Ebert L.,et al.Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.