fgf 17

Fibroblast Growth Factor 17 (FGF17) is a member of the heparin-binding growth factors family that is prominently expressed in the cerebellum and cortex. Proteins of this family possess broad mitogenic and cell survival activities and they are involved in a variety of biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth, and invasion. FGF17 plays an important role in the regulation of embryonic development and it acts as signaling molecule in the induction and patterning of the embryonic brain. In addition, FGF17 stimulates the proliferation and activation of cells that express FGF receptors.

FGF-13, also known as FGF17, belongs to the fibroblast growth factor (FGF) family. Members of this family show broad mitogenic and cell survival activities, and play a role in a variety of biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-13 is preferentially expressed in the embryonic brain. It interacts with FGFR3 and FGFR4. FGF-13 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is also required for normal brain development.

FGF-2 Protein, Human, Recombinant (K128N) is expressed in E. coli expression system. The predicted molecular weight is 17 KDa and the accession number is P09038-2.

Interleukin-17 receptor D (IL-17 RD), also known as SEF (similar expression to FGFs), is a type I transmembrane protein that is found in both the cytoplasm and plasma membrane. IL-17RD functions as a feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. It may inhibit FGF-induced FGFR1 tyrosine phosphorylation, regulate the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK By similarity, and mediate JNK activation and may be involved in apoptosis. IL-17RD interacts with the IL-17R downstream molecule TRAF6. It has been proposed that the IL-17RD intracellular domain interacts with IL-17R and TRAF6 to deliver the downstream signal.

FGF basic is one of 22 mitogenic proteins of the FGF family, which show 35-60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. The 17 kDa mouse sequence has 98% aa identity with rat, and 95% identity with human, bovine, and sheep FGF basic. Binding of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids with lower affinity. Expression of FGF basic is nearly ubiquitous but disruption of the mouse FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF family members. FGF basic modulates such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, neuronal function and neural degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and angiogenesis is reminiscent of a variety of pathological conditions.