磷酸化α-连环蛋白抗体

磷酸化α-连环蛋白抗体 Background: The distinct peripheral cytosolic proteins, alpha, beta and gamma-catenin (102, 94 and 86 kDa) found in many tissues bind to the conserved cytoplasmic tail domain of the cell-adhesion cadherins. Catenins link E-cadherin to other integral membrane or cytoplasmic proteins and are modulated by Wnt-1 proto-oncogene. They are good candidates for mediating transduction of cell-cell contact positional signals to the cell interior. Absence of alpha-catenin is found in certain tumor cell lines and reduced levels in certain human carcinomas. Beta-catenin binds directly to the cytoplasmic tail of E-cadherin. It binds to the N-terminus of alpha-catenin and interacts with the protein product of the tumor suppressor gene APC. This interaction involves a 15-aa repeat in the APC. Beta-catenin cell levels seem to be controlled by APC. The central core region of beta-catenin is involved in mediation of cadherin-catenin complex interaction with EGFR. Also known as: p-CTNNA1 (Ser641); CTNNA1 (phospho-Ser641); CTNNA1 (phospho-S641); alpha 1 Catenin (phospho S641); alpha catenin; alpha E catenin; alphaE catenin; Cadherin associated protein 102kDa; Cadherin associated protein; CAP 102; CAP102; Catenin (cadherin associated protein) alpha 1 102kDa; Catenin alpha 1; CTNNA 1; CTNNA1; Alpha-cats; FLJ36832; NY REN 13 antigen; CTNA1_HUMAN.磷酸化α-连环蛋白抗体