Recombinant human HSP60 protein

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.

Product Specifications

Product Name Alternative

Heat shock 60kDa protein 1, 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.

Expression System

E.coli

Antigen Species

Human

Tag

His-Tag

Applications

SDS-PAGE

Concentration

1 mg/mL (determined by Bradford assay)

Purity

> 95% by SDS-PAGE

Molecular Weight

63.2 kDa (593aa)

Additionnal Information

HSP60, Heat shock 60kDa protein 1, 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., HSP0802-10 µg, HSP0802-20 µg, HSP0802-50 µg, HSP0802-100 µg, HSP0802-250 µg, HSP0802-500 µg, HSP0802-1 mg, HSP0802-10, HSP0802-20, HSP0802-50, HSP0802-100, HSP0802-250, HSP0802-500, HSP0802-1

References & Citations

Cheng MY., et al. (1990), Nature. 348: 455- 458; ; Ghosh JC., et al. (2008), J Biol Chem. Feb 22; 283 (8) :5188-94

Other References

Kaiser F, et al. Monocyte cytokine synthesis in response to extracellular cell stress proteins suggests these proteins exhibit network behaviour. (Cell Stress Chaperones. 2014) {https://pubmed.ncbi.nlm.nih.gov/23775284/}

Storage Conditions

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Formulation

Liquid in. 25mM Tris-HCl buffer (pH 7.5) containing 100 mM NaCl, 5mM DTT, 10% glycerol

Scientific Category

Heat Shock Proteins

NCBI Accession Number

NP_002147.2

Uniprot Accession Number

P10809

Species

Human

AA Sequence

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