Analytical Data
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Gene name
TCP1
- Application
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Alternative Names
CCT-alpha; CCT1; CCTa; TCP-1-alpha; Chaperonin Containing TCP1, Subunit 1
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17987
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Expression Region
Gln276~Asp556
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Molecular Weight
61kDa
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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
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Protein Description
TCP1 (T-complex protein 1) is a vital molecular chaperone playing a crucial role in the folding of nascent proteins within the cell. As a component of the TCP1 ring complex (TRiC), it assists in the proper assembly and folding of a wide range of substrates, including cytoskeletal proteins and those involved in cellular signaling. Research into TCP1 has grown due to its implications in various biological processes and diseases; for instance, mutations or malfunctions in TCP1 have been associated with neurodegenerative disorders, cancer, and other pathologies. Understanding TCP1's structure, function, and interaction with client proteins is essential for elucidating its role in protein homeostasis and cellular stress responses. Moreover, TCP1 is a promising target for therapeutic interventions, as modulating its chaperoning activity could potentially correct protein misfolding and aggregation. The exploration of TCP1 also extends to its evolutionary significance, as it is highly conserved across many species, indicating its fundamental role in cellular function. Ongoing studies focus on the detailed mechanisms of TCP1-mediated protein folding, its regulatory pathways, and the development of novel strategies to harness its activity in biomedicine. This multifaceted approach not only enriches our understanding of cellular machinery but also opens avenues for innovative treatments for diseases linked to protein misfolding.
