Anti-FRAT1 (C-terminal region) antibody produced in rabbit

FRAT1 (frequently rearranged in advanced T-cell lymphomas-1) is a GSK3β binding protein consisting of a conserved GSK3β interacting domain. In human two FRAT genes have been identified, FRAT1 and FRAT2 whereas FRAT1-3 have been identified in mouse.

Anti-FRAT1 (C-terminal region) antibody is suitable for western blot at a concentration of 1-2μg/mL using rat liver extract (S1 fraction) and a HEK-293T cell lysate expressing human FRAT1.

By inhibiting GSK-3-mediated phosphorylation of β-catenin, FRAT1 plays a major role in the wnt-signaling pathway. During binding to the GSKβ3, it competes with axin and thus displacing GSKβ3 from the axin-β-catenin complex. In the canonical wnt signaling pathway, FRAT1 acts more efficiently than FRAT2. FRAT1 has correlation with clinicopathologic features. It has been reported that in several human malignant tumors, FRAT is overexpressed. It′s upregulated expression have been found in several human cancer lines such as gastric cancers and esophageal squamous cell carcinoma (ESCC).

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.