DATASHEET
Host:
Mouse
Target Protein:
δ1-Catenin (central region)
Specificity:
The antibody detects a 110 kDa* protein corresponding to the molecular mass of δ1-Catenin on SDS-PAGE immunoblots of human A431 and HUVEC cells.
Clonality:
Monoclonal
Isotype:
IgG1
Swiss Prot:
O60716
Source:
Clone (M354) was generated from a peptide that includes amino acids from the central region of human δ1-Catenin. This peptide sequence is highly conserved in rat and mouse δ1-Catenin.
Purification:
Purified by Protein A.
Storage Buffer:
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Storage:
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Background:
Catenins have emerged as molecular sensors that integrate cell-cell junctions and cytoskeletal dynamics with signaling pathways that control morphogenesis and cell to cell communication. δ1-Catenin (p120 catenin) is a catenin family member which contains an N-terminal coiled-coil domain, a regulatory domain containing multiple phosphorylation sites, and a central Armadillo repeat domain. δ1-Catenin regulates E-cadherin turnover, and has both positive and negative effects on cadherin-mediated adhesion. Actin dynamics are also regulated by δ1-Catenin, which can modulate RhoA, Rac and cdc42 activity. δ1-Catenin is phosphorylated at multiple tyrosine, serine and threonine sites both in vitro and in vivo. High levels of δ1-Catenin phosphorylated at Tyr-228 are commonly seen in several carcinoma cell lines and after EGFR activation. Many other tyrosine sites are also phosphorylated in the N-terminal region including Tyr-96, Tyr-112, Tyr-280, and Tyr-302. In addition, Thr-310 and Thr-916 are constituitively phosphorylated in many cell types, however this phosphorylation may occur only in δ1-Catenin associated with the plasma membrane.