Analytical Data
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Gene name
HSP60
- Application
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Alternative Names
60 kDa heat shock protein, mitochondrial; CPN60; HSP-60; HSPD1
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Species
Human
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Source
E. coli
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Tag
N-His;N-GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P10809-1
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Expression Region
L2-F573
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AA Sequence
LRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
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Protein Length
Partial
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Molecular Weight
52-88 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HSP60, or Heat Shock Protein 60, is a mitochondrial chaperonin that plays a crucial role in protein folding and assembly within the mitochondria. It is part of a larger family of heat shock proteins that are upregulated in response to stress, providing critical protection to cells by facilitating the proper folding of proteins and preventing the aggregation of misfolded proteins. Research on recombinant HSP60 has gained significant interest due to its potential implications in a variety of diseases, including neurodegenerative disorders, cancer, and autoimmune diseases. The production of recombinant HSP60 allows for the study of its structure and function in detail, paving the way for the development of therapeutic strategies targeting mitochondrial dysfunction. Moreover, HSP60 has been implicated in the immune response, serving not only as a chaperone but also as a modulator of inflammation and a potential biomarker for disease. Thus, the investigation of recombinant HSP60 is integral for understanding its multifaceted roles in health and disease, which could lead to novel diagnostic and therapeutic avenues in treating HSP60-related pathologies.
