Background

The protein encoded by this gene 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 two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found.

Images

	Western blotting analysis using anti-TCP1 antibody (Cat#63137). Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with anti-TCP1 antibody (Cat#63137, 1:5,000) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using FeQ™ ECL Substrate Kit (Cat#226).
	Western blotting analysis using anti-TCP1 antibody (Cat#63137). TCP1 expression in wild type (WT) and TCP1 shRNA knockdown (KD) HT-1080 cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with anti-TCP1 antibody (Cat#63137, 1:5,000) and HRP-conjugated goat anti-rabbit secondary antibody (Cat#201, 1:20,000) respectively. Image was developed using anti-NaQ™ ECL Substrate Kit (Cat#716).
	Flow cytometric analysis of TCP1 expression in HepG2 cells using anti-TCP1 antibody (Cat#63137, 1:2,000). Green, isotype control; red, TCP1.
	Immunocytochemical staining of HepG2 cells with anti-TCP1 antibody (Cat#63137, 1:1,000). Nuclei were stained blue with DAPI; TCP1 was stained magenta with Alexa Fluor® 647. Images were taken using Leica stellaris 5. Protein abundance based on laser Intensity and smart gain: High. Scale bar: 20 μm.

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