HSP10/EPF Protein, Human (His)

The HSP10/EPF protein is a cochaperone that plays a role in mitochondrial protein import and assembly. HSP10/EPF Protein, Human (His) is the recombinant human-derived HSP10/EPF protein, expressed by E. coli , with N-His, N-6*His labeled tag. The total length of HSP10/EPF Protein, Human (His) is 102 a.a., with molecular weight of ~13 KDa.

The HSP10/EPF protein functions as a co-chaperonin actively involved in mitochondrial protein import and macromolecular assembly. Collaborating with Hsp60, it facilitates the correct folding of imported proteins and, under stress conditions in the mitochondrial matrix, may prevent misfolding while promoting the refolding and proper assembly of unfolded polypeptides. The operational units of these chaperonins comprise heptameric rings of the large subunit Hsp60, forming a back-to-back double ring structure. In a cyclic process, Hsp60 ring complexes bind unfolded substrate proteins, followed by ATP binding and association with two heptameric rings of the co-chaperonin Hsp10. This leads to the sequestration of the substrate protein within the inner cavity of Hsp60, allowing for undisturbed folding. Synchronous ATP hydrolysis in all Hsp60 subunits results in the dissociation of the chaperonin rings, releasing ADP and the folded substrate protein. The HSP10/EPF protein forms a homoheptamer arranged in a ring structure and interacts with a Hsp60 tetradecamer to create the symmetrical football complex. These molecular interactions underscore the essential role of HSP10/EPF in orchestrating the folding and assembly of mitochondrial proteins.

Human

E. coli

P61604 (M1-D102)

3336  [NCBI]

MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD

Approximately 13 kDa.

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  Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 300 mM NaCl, 5% trehalose, 5% mannitol and 0.01% Tween 80, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.