PDZK1 Antibody

PDZ domains are protein interaction modules that are prevalent in various species, including bacteria, yeasts, plants, insects, and vertebrates . These domains are typically found in cytoplasmic proteins and are known for their role in binding either the carboxyl-terminal sequences of proteins or internal peptide sequences . PDZ domains are involved in numerous biological processes, such as transport, ion channel signaling, and other signal transduction systems .

PDZ domains consist of 80 to 90 amino acids, forming a compact globular structure with six beta-strands and two alpha-helices . The binding of ligands occurs in an elongated surface groove, where an anti-parallel beta-strand interacts with the beta-B strand and the B helix . This structure allows PDZ domains to bind to a free carboxylate group at the end of a peptide through a carboxylate-binding loop between the beta-A and beta-B strands .

PDZK1 is a scaffolding protein that contains four PDZ domains and plays a crucial role in the localization of cell surface proteins . It is particularly important in cholesterol metabolism by regulating the HDL receptor, scavenger receptor class B type 1 . The four PDZ domains in PDZK1 are located at amino acid positions 9-90, 134-215, 243-323, and 378-458 . Additionally, PDZK1 has two phosphorylation sites at Ser492 and Ser514 .

The mouse anti-human PDZK1 antibody is used in research to study the expression and function of PDZK1 in human cells. This antibody is valuable for investigating the role of PDZK1 in various cellular processes and its involvement in diseases related to cholesterol metabolism and other signaling pathways .