FGFR-1 alpha Protein, Human (Active, Biotinylated, sf9, Avi)

FGFR-1 alpha, a tyrosine-protein kinase, functions as a cell-surface receptor for fibroblast growth factors and plays a pivotal role in regulating embryonic development, cell proliferation, differentiation, and migration. It is essential for normal mesoderm patterning, proper axial organization during embryonic development, skeletogenesis, and the development of the gonadotropin-releasing hormone (GnRH) neuronal system. Upon ligand binding, FGFR-1 alpha activates multiple signaling cascades, phosphorylating key proteins such as PLCG1, FRS2, GAB1, and SHB. This activation leads to the production of signaling molecules like diacylglycerol and inositol 1,4,5-trisphosphate through PLCG1. Moreover, 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. FGFR-1 alpha also promotes the phosphorylation of SHC1, STAT1, and PTPN11/SHP2. Within the nucleus, it enhances the activity of RPS6KA1 and CREB1, contributing to the regulation of transcription. The down-regulation of FGFR-1 alpha signaling occurs through IL17RD/SEF and FGFR-1 alpha ubiquitination, internalization, and degradation.