FGF-10, Human
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KGF-2(also known as FGF-10) was originally identified from rat embryos by homology-based polymerase chain reaction. Human and mouse KGF-2 were subsequently cloned. The human KGF-2 cDNA encodes a 208 amino acid residue protein with a hydrophobic amino-terminal signal peptide. Human KGF-2 shares approximately 92% and 95% amino acid sequence identity with mouse and rat KGF-2, respectively. Among the FGF family members, KGF-2 is most closely related to FGF-7. The expression of KGF-2 transcripts has been shown to be most abundant in the embryo and adult lung. Recombinant KGF-2 preparations have been shown to be mitogenic for epithelial and epidermal cells but not fibroblasts. Based on its in vitro biological activities and in vivo expression pattern, KGF-2 has been proposed to play unique roles in the brain, in lung development, wound healing and limb bud formation.
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