TCP1 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of 2 identical stacked rings, each containing eight different proteins. Unfolded polypeptides penetrate the central cavity of the complex and are folded in an ATP-dependent manner. The TCP1 protein is found in the cytosol as a subunit of a hetero-oligomeric chaperone. TCP1 has a significant function in maintaining cellular homoeostasis by assisting the folding of many proteins such as the cytoskeletal components actin and tubulin.
DESCRIPTION
TCP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 576 amino acids (1-556 a.a.) and having a molecular mass of 62.5kDa. The TCP1 is purified by proprietary chromatographic techniques.
SOURCE
Escherichia Coli.
PHYSICAL APPEARANCE
Sterile Filtered colorless solution.
FORMULATION
The TCP1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 0.1mM PMSF and 10% Glycerol.
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.
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