Anti-FGFR-4 Antibody, clone 29.2 culture supernatant, clone 29.2, from rabbit

Fibroblast growth factor receptor 4 (UniProt: P22455; also known as EC: 2.7.10.1, FGFR-4, CD334) is encoded by the FGRF4 (also known as JTK2, TKF) gene (Gene ID: 2264) in human. FGFR-4 is a highly conserved, single-pass type I membrane protein with tyrosine kinase activity that serves as a cell surface receptor for fibroblast growth factors and regulates cell proliferation differentiation, and migration. FGFR-4 is expressed in gastrointestinal epithelial cells, pancreas, and gastric and pancreatic cancer cell lines. In the absence of a ligand, it is present as a monomer in an inactive conformation. Upon ligand binding it homodimerizes into an active conformation with autophosphorylation of tyrosine residues. FGFR-4 is synthesized with a signal peptide (aa 1-21), which is subsequently cleaved off in the mature form. It contains an extracellular domain (aa 22-369), a transmembrane domain (aa 370-390), and a cytoplasmic domain (aa 391-802). FGFR-4 undergoes N-glycosylation, and when not fully glycosylated it can undergo proteasomal degradation. FGFR-4 signaling is down-regulated by receptor internalization and degradation. MMP14 is reported to promote internalization and degradation of FGFR-4. Mutations that lead to constitutive kinase activation or impair normal FGFR-4 inactivation lead to aberrant signaling leading to tumor growth. (Ref.: Turkington, RC et al. (2014). Cell Death Dis. 5; e1046).