FGF13 Human
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
The FGF-13 is purified by proprietary chromatographic techniques.
Product Specs
Fibroblast growth factor 13 (FGF-13), a member of the extensive FGF family with over 23 members, is a binding growth factor. This family is characterized by a core 120 amino acid (aa) FGF domain, responsible for their shared tertiary structure. Human and mouse FGF13, consisting of 245 aa, are encoded by genes exhibiting alternative splicing at their N-termini. Several transcript variants have been observed in both species, encoding proteins of 245 aa, 199 aa, 226 aa, 192 aa, and 255 aa, with a high degree of cross-species amino acid identity (over 98%) across all isoforms. FGF13 expression is found in various tissues during fetal development, including the ependyma, dorsal root ganglia, cranial ganglia, both atrial and ventricular myocardium, and renal collecting duct-associated mesenchyme.
Product Science Overview
FGF13 is a protein-coding gene that plays a crucial role in various cellular processes. It shares 30-50% amino acid sequence identity with other FGFs and 60-70% identity with other members of the FGF11 subfamily . The primary structure of recombinant human FGF13 consists of a single polypeptide chain, which is biologically active and similar to its natural counterpart .
FGF13 is involved in the regulation of mitogenesis, differentiation, migration, angiogenesis, and wound healing . It activates signaling pathways such as the mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) pathway, which is crucial for cell proliferation . Interestingly, FGF13’s mitogenic effects are mediated by FGFRs, despite its classification as an intracrine protein .
Recombinant human FGF13 is typically produced using an Escherichia coli expression system. This method allows for large-scale production of the protein, which can then be purified using column chromatography . The recombinant protein is often produced in two isoforms, rhFGF13A and rhFGF13B, both of which are soluble when expressed in E. coli .
Recombinant FGF13 has significant applications in biomedical research. It is used to study cell signaling interactions and pathways, particularly those involved in cell proliferation and differentiation . FGF13’s ability to promote the proliferation of NIH3T3 cells in the presence of heparin highlights its potential in therapeutic applications .
Mutations or dysregulation of FGF13 have been associated with various diseases, including developmental and epileptic encephalopathy and intellectual developmental disorders . Understanding the molecular mechanisms of FGF13 can provide insights into these conditions and potentially lead to the development of targeted therapies.
