FGFR-2 beta (IIIb) Protein, Mouse (HEK293, His)

FGFR-2 beta, a tyrosine-protein kinase, operates as a cell-surface receptor for fibroblast growth factors, playing a pivotal role in the intricate regulation of cell proliferation, differentiation, migration, and apoptosis, as well as embryonic development. It is indispensable for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis, and skin development. Furthermore, FGFR-2 beta is crucial for the regulation of osteoblast differentiation, proliferation, and apoptosis, contributing significantly to normal skeleton development. While promoting cell proliferation in keratinocytes and immature osteoblasts, it induces apoptosis in differentiated osteoblasts. Through phosphorylation of PLCG1, FRS2, and PAK4, FGFR-2 beta initiates diverse signaling cascades upon ligand binding. Activation of PLCG1 leads to the production of diacylglycerol and inositol 1,4,5-trisphosphate. Additionally, phosphorylation of FRS2 triggers the recruitment of GRB2, GAB1, PIK3R1, and SOS1, mediating the activation of RAS, MAPK1/ERK2, MAPK3/ERK1, the MAP kinase signaling pathway, and the AKT1 signaling pathway. FGFR2 signaling is tightly regulated through ubiquitination, internalization, and degradation processes. Mutations disrupting normal maturation, internalization, or degradation of FGFR-2 lead to aberrant signaling, including constitutive kinase activation. Overexpression of FGFR-2 promotes the activation of STAT1.