FGFR3/CD333 Recombinant Rabbit

FGFR-3 protein is a tyrosine protein kinase that serves as a cell surface receptor for fibroblast growth factors, playing a pivotal role in the regulation of cell proliferation, differentiation, and apoptosis. It is crucial for cellular processes in chondrocytes, osteoblasts, and the inner ear development, and it also impacts normal bone development and postnatal bone mineralization. FGFR-3 protein is also prone to mutations, which can occur in a wide range of locations, classified into five mutation regions: A through E. These mutations can lead to various diseases, such as Muenke craniosynostosis syndrome, thanatophoric dysplasia, achondroplasia, Crouzon syndrome with acanthosis nigricans, and chondrodysplasia. Mechanistically, upon ligand binding, FGFR-3 activates multiple signaling cascades, including the phosphorylation of PLCG1, CBL, and FRS2. This activation leads to the production of cellular signaling molecules like diacylglycerol and inositol 1,4,5-trisphosphate. However, mutations that result in constitutively active kinase or impair normal FGFR3 maturation, internalization, and degradation can lead to aberrant signaling. Furthermore, overexpression or constitutive activation of FGFR3 can promote the activation of PTPN11/SHP2, STAT1, STAT5A, and STAT5B, further influencing cellular functions.