Human FGF R4-FcA Chimera

GWB-8E1A2C

FGF R4-FcB Chimera bound to protein A sepharose beads was able to pull down its ligand FGF-2. % Carbohydrate: purified FGF R4-FcB Chimera consists of 15-30% carbohydrate by weight. Glycosylation: FGF R4-FcB Chimera has N-linked and probably O-linked oligosaccharides.
Reconstitution: It is recommended that 0. 5 ml of sterile phosphate-buffered saline be added to the vial. Fibroblast growth factors (FGFs) belong to a large family (22 human members) of mitogenic factors ranging in molecular mass from 17-34 kDa. FGFs exhibit high affinity for heparin and heparin-like glycosaminoglycans (HLGAGs) and these interactions are required for signaling activation from the FGF receptors. FGFs are mitogens for fibroblasts and many other cell types and have additional cellular functions including effects on differentiation survival and motility. FGFs have major roles in hematopoiesis development wound repair angiogenesis and tumor growth. During embryonic development FGFs are involved in the formation of epithelial tissues organs and limbs. In adult organisms FGFs play a role in tissue repair and response to injury. The biological actions of FGFs are mediated through binding to the cognate FGF receptors which are members of the tyrosine kinase receptor family. Expression of FGF R4 is widespread and has been detected in the lung kidney adrenal liver pancreas intestine striated muscle and spleen tissues and particularly in fetal tissues. Multiple receptor splice variants produce a number of isoforms for each of the receptors. The FGF receptors are type I transmembrane cell surface proteins that comprise an extracellular domain (ECD) composed of three immunoglobulin-like (Ig) loops a transmembrane segment and an intracellular tyrosine kinase domain. Human fibroblast growth factor receptor 4 (FGF R4) is synthesized as an 802 amino acid glycoprotein that includes a 21 amino acid signal sequence a 348 amino acid ECD and a 412 amino acid cytoplasmic domain. The FGF R4 includes 2 potential N-linked glycosylation sites. For a recent review of signaling by FGF receptors please refer to Eswarakumar VP Lax I Schlessinger J. (2005) Cytokine Growth Factor Rev. 16(2): 139-49 and Ezzat S and Asa SL (2005) Horm Metab Res. 37(6):355-60.

Membrane; Single-pass type I membrane protein. Note=Isoform 2 may be secreted.

Glycosylated (By similarity). Phosphorylated on tyrosine residue (By similarity). Phosphorylation requires the presence of a functional (phosphorylated) FGFR1 and not necessarily by means of FGFR heterodimerization (By similarity).

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.