Recombinant Human G-CSF Receptor/CD114 (carrier-free)

Human G-CSF receptor (CSF3R) was initially isolated from the cDNA libraries of human U937 leukemia cells. The human G-CSF receptor is a type I cytokine receptor, possesses 836 amino acids, and has a clear homology (62.5%) with its murine counterpart. G-CSFR contains a conserved cytokine receptor homologous (CRH) domain, an Ig-like domain and three fibronectin type III-like domains in the extracellular region; a transmembrane region; and an intracellular region lacking intrinsic catalytic activity. Human G-CSF soluble receptor has been identified this form has a deletion of the transmembrane domain.  The complex G-CSF/G-CSFR has a 2:2 ligand:receptor stoichiometry. G-CSFR stimulates signals transduction proteins that induce granulocytic proliferation and differentiation such as the STAT 1, 3 and 5 transcription factors, the Ras/Mek/Erk1/2 pathway, the Src-related kinases Lyn and Hck, the serine/threonine kinase Akt, and the Syk tyrosine kinas. Also, G-CSFR is associated to pathways that negatively regulate granulopoiesis, including those mediated by the SHP-1 tyrosine phosphatase and the suppressor of cytokine signaling 3 (SOCS3) protein. Different mutations in the gene encoding the G-CSFR have been described with clinical consequences related to the myeloid lineage, including severe congenital neutropenia (SCN), myelodysplastic syndrome (MDS), acute myeloid leukemia (AML), and chronic neutrophilic leukemia (CNL).