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GroEL ( HSP60 ) Human Recombinant ( GroEL Human )
DescriptionRecombinant Human GroEL, HSP60 produced in E.Coli is a single, non-glycosylated polypeptide chain fused to a 20 a.a. His tag at N-terminus containing 593 amino acids (1-573 a.a.) and having a molecular mass of 63kDa.The HSP60 is purified
Data sheet
| Formulation | The GroEL protein contains 20mM Tris-HCl buffer pH-8.0, 5mM DTT and 10% Glycerol. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Description | Recombinant Human GroEL, HSP60 produced in E.Coli is a single, non-glycosylated polypeptide chain fused to a 20 a.a. His tag at N-terminus containing 593 amino acids (1-573 a.a.) and having a molecular mass of 63kDa.The HSP60 is purified by proprietary chromatographic techniques. |
| Protein Background | GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES coordinates the ATPase activity of the HSP60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding. |
| Expression host | Escherichia Coli. |
| Synonyms | CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa heat shock protein mitochondrial, Heat shock protein 60, HSP-60, 60 kDa chaperonin, Chaperonin 60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HuCHA60, HSPD1. |
| Reagent Appearance | Sterile filtered colorless solution. |
| Stability | Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. |
| Product Description | Immunoreactive with sera of HCV-infected individuals. |