|Application ||IF, WB, E|
|Other Accession||P63039, P63038, P18687, Q5ZL72, P31081|
|Predicted||Bovine, Chicken, Hamster, Mouse, Rat|
|Calculated MW||61055 Da|
|Antigen Region||187-215 aa|
|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|
|Target/Specificity||This HSPD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 187-215 amino acids from the Central region of human HSPD1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSPD1 Antibody (Center) 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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Provided below are standard protocols that you may find useful for product applications.
HSPD1 is a member of the chaperonin family. This protein may function as a signaling molecule in the innate immune system. The protein is essential for the folding and assembly of newly imported proteins in the mitochondria. The protein is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter.
References for protein:
1.Venner T.J., Singh B., Gupta R.S.DNA Cell Biol. 9:545-552(1990)
2.Hansen J.J., Bross P., Westergaard M., Nielsen M.N., Eiberg H.,Hum. Genet. 112:71-77(2003)
3.Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L.,Electrophoresis 18:588-598(1997)
4.Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.Biochem. J. 383:237-248(2004)
References for U251 cell line:
1. Westermark B.; Pontén J.; Hugosson R. (1973).” Determinants for the establishment of permanent tissue culture lines from human gliomas”. Acta Pathol Microbiol Scand A. 81:791-805. [PMID: 4359449].
2. Pontén, J.,Westermark B. (1978).” Properties of Human Malignant Glioma Cells in Vitro”. Medical Biology 56: 184-193.[PMID: 359950].
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