Recombinant Human Hsp60 protein
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Recombinant Human Hsp60 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.
View Alternative Names
HSP60, HSPD1, 60 kDa chaperonin, Chaperonin 60, Heat shock protein 60, Heat shock protein family D member 1, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, CPN60, HSP-60, Hsp60
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Hsp60 protein (AB56277)
SDS-PAGE analysis of ab56277 with molecular weight markers. Approximate molecular weight 85kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The protein ensures mitochondrial protein stability by facilitating the refolding of misfolded proteins and cooperating with other chaperonins like Hsp10. Hsp60 participates in forming a complex with these proteins to create a conducive environment for protein folding. It plays a part in regulating mitochondrial homeostasis impacting cell survival and apoptosis processes.
Pathways
Hsp60 links to the ATP synthesis and apoptosis pathways showcasing its importance as a mitochondrial marker. It interacts with proteins like caspase-3 to modulate cell death mechanisms highlighting its influence beyond simple protein folding. In the ATP synthesis pathway it contributes indirectly to energy production by maintaining mitochondrial function.
Specifications
Form
Liquid
General info
Function
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, 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 : 11422376, PubMed : 1346131). 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).
Sequence similarities
Belongs to the chaperonin (HSP60) family.
Subcellular localisation
Mitochondrion matrix
Target data
Alternative Products
Complementary Products
Primary Antibodies
AB46798
Anti-Hsp60 antibody - Mitochondrial Marker
BOND RX™ Validated|Lab Essentials
- 5
- 13
Product promise
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