Analytical Data
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Gene name
CCT2
- Application
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Alternative Names
CCT-beta
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P78371
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Expression Region
2-535aa
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Molecular Weight
73.4 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
CCT2, or Chaperonin Containing TCP1 Subunit 2, is a key member of the CCT (Chaperonin Containing TCP1) complex, which plays a critical role in the proper folding of cytosolic proteins, particularly those involved in the assembly of multi-subunit proteins. The significance of CCT2 in cellular processes has drawn attention due to its involvement in critical functions such as protein homeostasis, cellular stress responses, and regulation of cell growth. Abnormalities in CCT2 have been implicated in various diseases, including cancer and neurodegenerative disorders, making it a potential target for therapeutic interventions. Research on CCT2 recombinant proteins involves elucidating its structure, function, and interactions within the cellular environment, as well as its role in pathology. Understanding the biochemical properties of CCT2, including its interaction with client proteins and other chaperones, can provide insights into molecular mechanisms of disease and aid in the development of novel therapeutic strategies. Moreover, the production of recombinant CCT2 proteins in model systems allows for comprehensive studies on its folding mechanisms and functional dynamics, ultimately contributing to a greater understanding of protein misfolding diseases. Overall, research on CCT2 and its recombinant forms is vital for advancing the knowledge of protein biology and for the potential development of therapeutic approaches targeting its associated pathways.
