描述：
Stem cell factor (SCF), also known as c-kit ligand (KL), mast cell growth factor (MGF), and
steel factor (SLF), is a widely expressed 2840 kDa type I transmembrane glycoprotein. It
promotes the survival, differentiation, and mobilization of multiple cell types including
myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors. SCF
is a primary growth and activation factor for mast cells and eosinophils. Mature human SCF
consists of a 189 amino acid (aa) extracellular domain (ECD), a 23 aa transmembrane segment,
and a 36 aa cytoplasmic tail. The ECD shows both N-linked and O-linked glycosylation.
Proteolytic cleavage at two alternate sites in the extracellular juxtamembrane region releases
a 25 kDa soluble molecule which is comparable to the only form produced by Steeldickie
mutant mice. An alternately spliced isoform of human SCF lacks 28 aa that encompasses the
primary proteolytic recognition site. Within the ECD of the long isoform (corresponding to this
recombinant protein), human SCF shares 79%-87% aa sequence identity with canine, feline,
mouse, and rat SCF. Rat SCF is active on mouse and human cells, but human SCF is only weakly
active on mouse cells. Noncovalent dimers of transmembrane or soluble SCF interact with the
receptor tyrosine kinase SCF R/c-kit to trigger receptor dimerization and signaling. SCF assists
in the recovery of cardiac function following myocardial infarction by increasing the number
of cardiomyocytes and vascular channels.
原厂资料：
Stem cell factor (SCF), also known as c-kit ligand (KL), mast cell growth factor (MGF), and
steel factor (SLF), is a widely expressed 2840 kDa type I transmembrane glycoprotein. It
promotes the survival, differentiation, and mobilization of multiple cell types including
myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors. SCF
is a primary growth and activation factor for mast cells and eosinophils. Mature human SCF
consists of a 189 amino acid (aa) extracellular domain (ECD), a 23 aa transmembrane segment,
and a 36 aa cytoplasmic tail. The ECD shows both N-linked and O-linked glycosylation.
Proteolytic cleavage at two alternate sites in the extracellular juxtamembrane region releases
a 25 kDa soluble molecule which is comparable to the only form produced by Steeldickie
mutant mice. An alternately spliced isoform of human SCF lacks 28 aa that encompasses the
primary proteolytic recognition site. Within the ECD of the long isoform (corresponding to this
recombinant protein), human SCF shares 79%-87% aa sequence identity with canine, feline,
mouse, and rat SCF. Rat SCF is active on mouse and human cells, but human SCF is only weakly
active on mouse cells. Noncovalent dimers of transmembrane or soluble SCF interact with the
receptor tyrosine kinase SCF R/c-kit to trigger receptor dimerization and signaling. SCF assists
in the recovery of cardiac function following myocardial infarction by increasing the number
of cardiomyocytes and vascular channels.
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