β-TrCP Recombinant Rabbit mAb (S-3941-63)

β-TrCP (beta-transducin repeat-containing protein, also known as FBXW1 or BTRC) is a key F-box substrate recognition subunit of the SCF (SKP1-Cullin1-F-box) E3 ubiquitin ligase complex. Its core structure consists of multiple WD40 repeats that form a propeller-like beta-propeller structure, responsible for specifically recognizing and binding to the phosphorylated degron motif (typically "DSGxxS" or "DSGxxT," where the serine/threonine residues require pre-phosphorylation by kinases) in substrate proteins. Through this phosphorylation-dependent recognition mechanism, β-TrCP mediates the ubiquitination and subsequent degradation of various key signaling molecules—such as β-catenin, IκBα, Snail, Claspin, and CDC25A—thereby broadly regulating core signaling pathways including Wnt/β-catenin, NF-κB, Hedgehog, and cell cycle checkpoints. Physiologically, β-TrCP participates in maintaining normal cell cycle progression, DNA damage repair, cell polarity, and epithelial-mesenchymal transition (EMT). Pathologically, its aberrant expression or mutations are closely associated with the development and progression of various malignancies (such as colorectal cancer, breast cancer, and hepatocellular carcinoma). It can function as a tumor suppressor by degrading oncogenic proteins, but under certain circumstances, it may also promote cancer progression by degrading tumor suppressors, exhibiting its complex dual regulatory functions.