FGF-10 Protein, Human

Catalog Number: UA040565 Brand: UA BIOSCIENCE

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$160 USD

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Product Details

Product Specification

Species	Human
Synonyms	Fibroblast growth factor 10, FGF-10, Keratinocyte growth factor 2
Accession	O15520
Amino Acid Sequence	Gln38-Ser208
Expression System	E.coli
Molecular Weight	19-21 kDa (Reducing)
Purity	>95% by SDS-PAGE & HPLC.
Endotoxin	<0.1EU/μg
Conjugation	Unconjugated
Tag	No Tag
Physical Appearance	Lyophilized powder
Storage Buffer	PBS, pH7.4
Reconstitution	Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability & Storage	·12 months from date of receipt, lyophilized powder stored at -20 to -80℃. ·3 months, -20 to -80℃ under sterile conditions after reconstitution. ·1 week, 2 to 8℃ under sterile conditions after reconstitution. ·Please avoid repeated freeze-thaw cycles.
Reference	Front Genet. 2018 Sep 25;9:418. Sci Rep. 2016 Feb 12;6:21642.

Background

Fibroblast Growth Factor 10 (FGF-10), also known as Keratinocyte Growth Factor 2 (KGF-2), is a member of the fibroblast growth factor (FGF) family, specifically belonging to the FGF7 subfamily. Human FGF-10 is a 19 kDa protein composed of 208 amino acids, encoded by the FGF10 gene located on chromosome 5p13-p12. It was first isolated from human lung cDNA libraries by Emoto et al. in 1997 and subsequently characterized as a paracrine signaling molecule with structural homology to FGF-7 (KGF).

Unlike endocrine FGFs, FGF-10 functions as a paracrine signaling factor that requires heparan sulfate proteoglycans as essential co-factors for high-affinity binding to its cognate receptor. FGF-10 exhibits high specificity for the FGFR2-IIIb splice variant (also known as FGFR2b or K-sam), which is predominantly expressed in epithelial cells. This ligand-receptor interaction is critical for mediating mesenchymal-epithelial communication during development and tissue homeostasis.

Structurally, FGF-10 contains a conserved β-trefoil core domain characteristic of the FGF family, along with unique N-terminal and C-terminal extensions that influence its receptor binding specificity and biological activity. The protein is secreted through the classical endoplasmic reticulum-Golgi pathway and undergoes proteolytic processing to generate the mature, biologically active form.