FGFR-4 Protein, Human (Biotinylated, HEK293, His)

The FGFR-4 protein is a tyrosine protein kinase and cell surface receptor for fibroblast growth factor that regulates diverse cellular processes such as proliferation, differentiation, migration, lipid metabolism, and bile acid biosynthesis. Notably, it contributes to the downregulation of the bile acid synthase CYP7A1 in response to FGF19. FGFR-4 Protein, Human (Biotinylated, HEK293, His) is the recombinant human-derived FGFR-4 protein, expressed by HEK293 , with C-His labeled tag.

FGFR-4 protein is a tyrosine-protein kinase that functions as a cell-surface receptor for fibroblast growth factors. It plays a crucial role in regulating cell proliferation, differentiation, migration, lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism, and phosphate homeostasis. One of its important functions is to facilitate the down-regulation of CYP7A1, the key enzyme in bile acid synthesis, in response to FGF19. Upon ligand binding, FGFR-4 phosphorylates PLCG1 and FRS2, leading to the activation of various signaling cascades. This activation results in the production of diacylglycerol and inositol 1,4,5-trisphosphate, which are important cellular signaling molecules. Additionally, phosphorylation of FRS2 triggers the recruitment of GRB2, GAB1, PIK3R1, and SOS1, leading to the activation of RAS, MAPK1/ERK2, MAPK3/ERK1, and the AKT1 signaling pathway. FGFR-4 also promotes the SRC-dependent phosphorylation of MMP14, a matrix protease, and facilitates its lysosomal degradation. The signaling of FGFR-4 is tightly regulated through receptor internalization and degradation, and MMP14 aids in this process. However, mutations that result in constitutive kinase activation or impair normal FGFR-4 inactivation can lead to aberrant signaling.

Human

HEK293

C-His

P22455-1 (L22-D369)

2264  [NCBI]

Approximately 60.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.