CGI-58 Antibody

CGI-58 antibody is directed against an amino acid sequence within the C-terminus of human CGI-58. The human genome encodes 19 distinct CGI-58 genes and 15 amino acid variants, but their function is unclear. CGI-58 is phosphorylated in the presence of ATP and in vitro, suggesting that it may be a substrate of the phosphatase PKA. It has been shown to interact with several proteins, including LC3, a key component of autophagy. CGI-58 overexpression decreases cellular TG accumulation in fibroblasts from CDS patients and stimulates mitophagy under basal conditions in cultured cells, but not in the absence of ATP (Fig. 6A). To directly examine a role for CGI-58 in autophagosome formation, we overexpressed the human LC3-GFP fusion protein in stable cell lines and treated them with bafilomycin A1. We observed that phosphorylation of CGI-58 affects LC3 recruitment to mitochondria, which is confirmed by confocal microscopy of LC3-GFP-positive autophagosomes (Fig. 7B).

CGI-58 antibody its orthologs exhibit a wide range of biochemical functions, most notably the ability to regulate lipolysis in adipose tissues and the capacity to form complexes with acyl-CoA for the synthesis of lipid mediators involved in signaling pathways. The acyl-CoA dependent LPAAT activity and the ATGL activation are shared features of CGI-58 in different vertebrates, but other biochemical functions are tissue specific.

CGI-58 Antibody: Applications and Research Benefits

The N-terminal domain and the cap of CGI-58 share only a low percentage of identity among vertebrates, while the catalytic Asp is highly conserved. Thus, the cap might play a pivotal role in controlling the specificity and positioning of substrates in a potential binding pocket. This conclusion is supported by the fact that mutations of corresponding residues in the a/b hydrolase fold lead to loss of substrate recognition and activity.