Analytical Data
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Gene name
CORT
- Application
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Alternative Names
CORT；Cortistatin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00230
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Expression Region
1-105aa
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AA Sequence
MPLSPGLLLLLLSGATATAALPLEGGPTGRDSEHMQEAAGIRKSSLLTFLAWWFEWTSQASAGPLIGEEAREVARRQEGAPPQQSARRDRMPCRNFFWKTFSSCK
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Molecular Weight
11.5 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
CORT, or C-terminal of Hsp70-interacting protein, is a crucial component in the regulation of cellular stress responses, particularly in the context of heat shock protein (Hsp70) interactions. The study of CORT-recombinant proteins has garnered attention due to their potential implications in understanding and treating various diseases, including neurodegenerative disorders and cancers, where Hsp70 plays a significant role in protein folding and protection against cellular stress. CORT operates by modulating the Hsp70 chaperone's activity, influencing cellular repair mechanisms, protein aggregation, and apoptosis pathways. Researchers are interested in elucidating the structure-function relationship of CORT to decipher its specific interactions within the Hsp70 complex and its effects on cellular homeostasis. Recombinant protein technology enables the production of CORT in controlled environments for functional studies, high-throughput screening, and the development of therapeutic agents aimed at modulating Hsp70 activity. Additionally, understanding CORT's role in stress responses can provide insights into the molecular mechanisms underlying various pathologies, making it a target of interest for pharmacological research and the development of novel therapies. The growing body of research surrounding CORT highlights its significance in cellular biology and its potential applications in medical science.
