|Application ||WB, IHC, FC, ICC, E|
|Reactivity||Human, Mouse, Rat, Monkey|
|Description||This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. (provided by RefSeq)|
|Immunogen||Purified recombinant fragment of human HSP60 expressed in E. Coli. |
|Formulation||Ascitic fluid containing 0.03% sodium azide.|
|Other Names||60 kDa heat shock protein, mitochondrial, 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, Hsp60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1, HSP60|
WB~~1/500 - 1/2000
IHC~~1/200 - 1/1000
IF~~1/200 - 1/1000
FC~~1/200 - 1/400
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP60 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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: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.|
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