| Product Name | HSP60, 27-573aa, Human |
|---|---|
| Description | HSP60 is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Recombinant human HSP60 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | 60 kDa heat shock protein, mitochondrial, CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13 |
| Host | E. coli |
| Molecular Weight | 26.6 kDa (232aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMAKDVK FGADARALML QGVDLLADAV AVTMGPKGRT VIIEQSWGSP KVTKDGVTVA KSIDLKDKYK NIGAKLVQDV ANNTNEEAGD GTTTATVLAR SIAKEGFEKI SKGANPVEIR RGVMLAVDAV IAELKKQSKP VTTPEEIAQV ATISANGDKE IGNIISDAMK KVGRKGVITV KDGKTLNDEL EIIEGMKFDR GYISPYFINT SKGQKCEFQD AYVLLSEKKI SSIQSIVPAL EIANAHRKPL VIIAEDVDGE ALSTLVLNRL KVGLQVVAVK APGFGDNRKN QLKDMAIATG GAVFGEEGLT LNLEDVQPHD LGKVGEVIVT KDDAMLLKGK GDKAQIEKRI QEIIEQLDVT TSEYEKEKLN ERLAKLSDGV AVLKVGGTSD VEVNEKKDRV TDALNATRAA VEEGIVLGGG CALLRCIPAL DSLTPANEDQ KIGIEIIKRT LKIPAMTIAK NAGVEGSLIV EKIMQSSSEV GYDAMAGDFV NMVEKGIIDP TKVVRTALLD AAGVASLLTT AEVVVTEIPK EEKDPGMGAM GGMGGGMGGG MF |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.4M UREA, 10% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Cappello F, Di Stefano A, et al. (2006). Cancer. 107(10):2417-24. |
| Background | HSP60 is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Recombinant human HSP60 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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