Cct8 (NM_009840) Mouse Recombinant Protein

Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.[UniProtKB/Swiss-Prot Function]

Purified recombinant protein of Mouse chaperonin containing Tcp1, subunit 8 (theta) (Cct8), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug

Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.