Abcam, ab161051, Recombinant Human TCP1 eta protein

Size: 10µg
Recombinant Human TCP1 eta protein is a Human Full Length protein, in the 1 to 543 aa range, expressed in Wheat germ, suitable for ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:WB, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q99832,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.31% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The TCP1 eta protein alternatively known as CCT7 is a molecular chaperone involved in protein folding. It is a component of the eukaryotic chaperonin complex known as the T-complex protein 1 (TCP1) ring complex (TRiC). The protein has an approximate mass of 58 kDa and is widely expressed across various tissues. TCP1 eta forms a multi-subunit structure in cells where it assists in the proper folding of newly synthesized polypeptides particularly actin and tubulin.
Biological function summary
TCP1 eta functions as part of the chaperonin-containing TCP1 (CCT) complex. The CCT complex plays a critical role in maintaining cellular proteostasis by promoting the correct folding and assembly of proteins. Ths complex is key for regulatory processes in the cytoskeleton and cell cycle. The folding activity of TCP1 eta is essential for cytoskeletal dynamics given its involvement with structural proteins like actin.
Pathways
TCP1 eta engages significantly in the actin and tubulin folding pathways. These pathways are vital for the formation of the cytoskeleton and spindle apparatus which are necessary for cell shape and division. TCP1 eta interacts with other chaperonin proteins such as TCP1 epsilon within these pathways to ensure efficient folding and stability of target proteins.
TCP1 eta has been linked to certain neurodegenerative diseases and cancer. Misfolded proteins are often associated with conditions like Huntington's disease where impaired CCT function disrupts protein homeostasis. Additionally there are connections between TCP1 eta and the stability of oncogenic proteins implicating its role in cancer progression. Interactions with other proteins such as p53 are relevant for understanding its role in these disease contexts.