描述：
Feline SCF (stem cell factor; also known as c-kit ligand) is a type I transmembrane (TM)
glycoprotein that plays an important role in a number of fetal and adult developmental
processes. It is synthesized as a 274 amino acid (aa) precursor that contains a 25 aa signal
sequence, a 190 aa extracellular region, a 23 aa TM segment and a 36 aa cytoplasmic tail.
Within the extracellular region there are two intrachain disulfide bonds and four α-helices.
Although the predicted molecular weight is 19 kDa, the native molecule is anywhere from
28 40 kDa in size and reflects both N and Olinked glycosylation. Glycosylation is not
necessary for bioactivity. The transmembrane form of SCF can be cleaved proteolytically,
generating a 165 aa soluble form. Circulating SCF exists as both a monomer and
nondisulfidelinked homodimer, with monomer predominating (50% to 75%). Both the
soluble and TM forms have bioactivity. Their principal targets may be different, however. A
second, alternate splice short form of feline SCF has been identified. It too, is membrane
bound and contains 246 aa residues. It will not give rise to a soluble form, since alternate
splicing removes the proteolytic cleavage site used in the long form. The ratio of long form
to short form varies tissue to tissue. Soluble feline SCF shares 93%, 93%, 90%, 87%, and 78%
aa sequence identity with porcine, canine, bovine, human and mouse SCF, respectively. Cells
known to express SCF include endothelial cells, fibroblasts and keratinocytes.
原厂资料：
Feline SCF (stem cell factor; also known as c-kit ligand) is a type I transmembrane (TM)
glycoprotein that plays an important role in a number of fetal and adult developmental
processes. It is synthesized as a 274 amino acid (aa) precursor that contains a 25 aa signal
sequence, a 190 aa extracellular region, a 23 aa TM segment and a 36 aa cytoplasmic tail.
Within the extracellular region there are two intrachain disulfide bonds and four α-helices.
Although the predicted molecular weight is 19 kDa, the native molecule is anywhere from
28 40 kDa in size and reflects both N and Olinked glycosylation. Glycosylation is not
necessary for bioactivity. The transmembrane form of SCF can be cleaved proteolytically,
generating a 165 aa soluble form. Circulating SCF exists as both a monomer and
nondisulfidelinked homodimer, with monomer predominating (50% to 75%). Both the
soluble and TM forms have bioactivity. Their principal targets may be different, however. A
second, alternate splice short form of feline SCF has been identified. It too, is membrane
bound and contains 246 aa residues. It will not give rise to a soluble form, since alternate
splicing removes the proteolytic cleavage site used in the long form. The ratio of long form
to short form varies tissue to tissue. Soluble feline SCF shares 93%, 93%, 90%, 87%, and 78%
aa sequence identity with porcine, canine, bovine, human and mouse SCF, respectively. Cells
known to express SCF include endothelial cells, fibroblasts and keratinocytes.
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