SCF was first identified as a growth factor essential for the survival, proliferation, and differentiation of hematopoietic stem cells and progenitor cells . It is produced by various cell types, including endothelial cells, fibroblasts, keratinocytes, gut epithelial cells, and tumor cells . SCF can exist both as a transmembrane protein and a soluble protein .
The human recombinant form of SCF is a non-glycosylated protein containing 165 amino acids and has a molecular mass of 18.4 kDa . It is typically produced in Escherichia coli (E. coli) and is available in a lyophilized (freeze-dried) form for research purposes .
SCF exerts its biological effects by binding to the c-Kit receptor (CD117), a type of receptor tyrosine kinase . This interaction triggers a cascade of intracellular signaling pathways that regulate various cellular processes, including:
Recombinant human SCF is widely used in research to study its effects on various cell types and to understand its role in different biological processes. It is also used in cell culture systems to support the growth and maintenance of hematopoietic stem cells .
In addition to its role in normal physiology, SCF has been implicated in various pathological conditions. For example, some tumor cells produce SCF, which can promote their proliferation and invasiveness . Understanding the mechanisms by which SCF influences these processes is an area of active research.