|FRAT2 in NTera‑2 Human Cell Line. FRAT2 was detected in immersion fixed NTera‑2 human testicular embryonic carcinoma cell line cultured with (left panels) and without (right panels) 10μM retinoic acid for 4 days using Sheep Anti-Human FRAT2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7980) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (red, upper panels; Catalog # NL010) and counterstained with DAPI (blue, lower panels). Specific staining was localized to nuclei. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
FRAT2 (Frequently Rearranged in Advanced T-cell lymphomas-2; also GSK-3-binding protein FRAT2) is an intracellular member of the GSK-3-binding protein family. Although its predicted MW is 28 kDa, due to its highly acidic nature, it runs anomalously at 35 kDa in SDS-PAGE. It is widely expressed, and plays a key role in the regulation of the Wnt signaling pathway. Typically, in the absence of stimulation, GSK-3 beta and beta -catenin associate with Axin, where GSK-3 beta phosphorylates beta -catenin, leading to its turnover. Upon Wnt stimulation, GSK-3 beta phosphorylation of beta -catenin is decoupled, resulting in beta -catenin mediated gene activation. FRAT2 has the same effect as Wnt stimulation on GSK-3 beta activity, serving as a non-Wnt activator of beta -catenin. It does so by promoting the dissociation of GSK-3 beta from axin. It also interacts with Diversin, a participant in JNK signaling. This suggests that FRAT2 plays a role in both Wnt/ beta -catenin and PCP signaling pathways. Human FRAT2 is 233 amino acids (aa) in length. It contains an N-terminal acidic domain (aa 1-54), a Pro-rich segment (aa 60-107) and a GSK-3 beta binding region (aa 171-196). Over aa 31‑233, human FRAT2 shares 73% aa sequence identity with both mouse FRAT2 and human FRAT1.