G-CSF-R (E8E7D) Rabbit mAb recognizes endogenous levels of total G-CSF-R protein.

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the extracellular domain of human G-CSF-R protein.

Granulocyte colony-stimulating factor receptor (G-CSF-R) is a transmembrane protein composed of an immunoglobulin-like (Ig-like) domain, a cytokine receptor-homologous (CRH) domain, and three fibronectin type III (FNIII) domains (1). G-CSF-R is expressed on all granulocytic lineages, including progenitor cells, and has been detected on monocytes, T and B lymphocytes, as well as non-hematopoietic tissues, including cardiomyocytes and neural stem cells (2-6). The primary ligand for G-CSF-R is the cytokine granulocyte colony-stimulating factor (G-CSF). G-CSF-R has no intrinsic tyrosine kinase activity; ligand binding induces conformational changes in the receptor, leading to activation of the Jak/Stat, PI3K/Akt, and MAPK pathways (7-10). G-CSF induces differentiation and proliferation of myeloid progenitor cells into neutrophils (11). Multiple diseases have been associated with mutations of the G-CSF-R gene, CSF3R, including severe congenital neutropenia (SCN), chronic neutrophilic leukemia (CNL), and atypical chronic myeloid leukemia (aCML) (12).