Recombinant Human SCF (His, Flag)

Stem cell factor (SCF) is a potent hematopoietic growth factor required to regulate embryonic and adult artificial blood. SCF proteins promote survival, differentiation, and mobilization in a variety of cell types, including myeloid cells, erythrocytes, megakaryocytes, lymphocytes, germ cells, and melanocyte progenitor cells. SCF is the primary growth and activation factor for mast cells and eosinophils. SCF contributes to the recovery of cardiac function after myocardial infarction by increasing the number of cardiomyocytes and vascular channels. Stem cell factor is an important ex vivo clinical application cytokine. SCF is used along with other cytokines for the culture and expansion of hematopoietic stem cells (HSCs), as well as for the proliferation and differentiation of myeloid and erythroid progenitor cells. Mature stem cell factors are composed of an extracellular domain (ECD) of 189 amino acids (aa), a transmembrane domain of 23 amino acids, and a cytoplasmic tail of 36 amino acids. ECD shows N-linked and O-linked glycosylation. SCF proteins are available in two forms, one that is membrane-bound and the other is a soluble form that lacks proteolytic treatment of the transmembrane domain and cytoplasmic tail. The soluble form is produced by proteolytic cleavage at two alternating sites in the extracellular proximal membrane region, releasing a soluble SCF protein of 25 kDa, which is comparable to the only form produced by Steel-dickie mutant mice. There is also an alternate splicing isoform of human SCF that lacks the 28 amino acids that contain major proteolytic recognition sites.