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SCF, a hematopoietic growth factor, functions by activating the c-Kit receptor. This interaction is crucial for the survival, proliferation, and differentiation of hematopoietic cells committed to melanocyte and germ cell lineages. Interestingly, Human SCF has limited activity on murine cells, whereas murine and rat SCF are fully functional on Human cells.
The Human SCF gene encodes a 273 amino acid transmembrane protein, consisting of a 25 amino acid N-terminal signal sequence, a 189 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 36 amino acid cytoplasmic domain. The soluble form of SCF is produced by proteolytic cleavage of the membrane-anchored precursor.
Recombinant Human SCF is an 18.4 kDa polypeptide comprising 165 amino acid residues, representing the sequence of the secreted soluble form of SCF.
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