| Product Name | HSP60, 1-573aa, Human, Recombinant |
|---|---|
| Description | Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. HSP60 is the ~60kDa mammalian equivalent to GroEL of E.coli. Process of HSP60 is regulated by the cochaperonin HSP10, a single heptameric ring of ~10kD subunits that forms a complex with HSP60. HSP10 coordinates the ATPase activity of the HSP60 subunits to allow the release of bound polypeptide in a manner productive for folding. Recombinant human HSP60, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | CPN60, GroEL, HSP65, SPG13, HuCHA60, Heat shock 60kDa protein 1, HSP60, Heat shock 60kDa protein 1 60 kDa chaperonin, GroEL, E, coli, homolog of, 60 kDa heat shock protein mitochondrial, 60kDa, cb863, Chaperonin, Chaperonin 60, Chaperonin, 60-KD, CPN 60, fa04a05, fb22d10, fi27b05, GroEL Homolog, Heat shock 60kD protein 1 (chaperonin), Heat shock 60kD protein 1 chaperonin, heat shock 60kDa protein 1 (chaperonin), Heat shock protein 1 (chaperonin), Heat Shock Protein 60, Heat shock protein 65, HLD4, Hsp 60, HSP 65, HSPD 1, HSPD1, HuCHA60, id:ibd2197, Spastic paraplegia 13 Mitochondrial matrix protein P1, P60 lymphocyte protein, sb:cb144, Short heat shock protein 60 Hsp60s1, Spastic paraplegia 13 (autosomal dominant), SPG 13, wu:fa04a05, wu:fb22d10, wu:fi04a12, wu:fi27b05. |
| Host | E. coli |
| Molecular Weight | 21.1kDa (189aa), confirmed by MALDI-TOF. |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris pH 7.5, 2mM EDTA |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 95% 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 | Cheng MY., et al. (1990), Nature. 348: 455- 458 Ghosh JC., et al. (2008), J Biol Chem. Feb 22; 283(8):5188-94 |
| Background | Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. HSP60 is the ~60kDa mammalian equivalent to GroEL of E.coli. Process of HSP60 is regulated by the cochaperonin HSP10, a single heptameric ring of ~10kD subunits that forms a complex with HSP60. HSP10 coordinates the ATPase activity of the HSP60 subunits to allow the release of bound polypeptide in a manner productive for folding. Recombinant human HSP60, 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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