Human CD117/c-kit PE-conjugated Antibody

Stem Cell Factor Receptor (CD117, the gene product of the c-kit proto-oncogene) and its ligand, Stem Cell Factor (SCF), also known as c-kit Ligand, Mast Cell Growth Factor, play essential roles in gametogenesis, melanogenesis, and hematopoiesis. The human SCF Receptor cDNA encodes a 972 amino acid (aa) residue precursor membrane protein with a 25 aa residue signal peptide (experimentally determined), a 495 aa residue extracellular domain, a 23 aa residue transmembrane segment, and a 429 aa residue cytoplasmic domain. SCF Receptor is a member of the type III subfamily of Receptor Tyrosine Kinases (RTK) that also includes the receptors for M-CSF, Flt-3, PDGF, and VEGF. All class III RTKs are characterized by the presence of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. SCF binding induces receptor homodimerization and signal transduction. SCF Receptor is expressed in hematopoietic progenitor cells, normal B and T lymphocyte progenitor cells, mast cells, germ cells, melanocytes, neurons, glial cells, placenta, kidney, lung, and gut. In addition, SCF Receptor expression has also been reported in a number of human tumor cell lines. SCF Receptor can be proteolytically cleaved from the cell surface and high levels of soluble SCF Receptor has been detected in cell conditioned medium and human plasma. Recombinant soluble SCF Receptor binds SCF with high affinity and is a potent SCF antagonist.