金山科研平台，产品价格货期咨询微信：jinshanbio Source:E. coli-derived, Glu33-Ser190, with an N-terminal Met Accession #:NP_757350 N-terminal Sequence Analysis:Met Structure:Disulfide-linked homodimer Purity:>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin Level:< 0.01 EU per 1 μg of the protein by the LAL method. Predicted Molecular Mass:18.5 kDa (monomer) SDS-PAGE:37 kDa, non-reducing conditions Activity:Measured in a cell proliferation assay using M‑NFS‑60 mouse myelogenous leukemia lymphoblast cells. Halenbeck, R. et al. (1989) Biotechnology 7:710. The ED₅₀ for this effect is typically 0.5-1.5ng/mL. Formulation:Lyophilized from a 0.2 µm filtered solution in PBS.See Certificate of Analysis for details. Molecule Information: M-CSF Long Name: Macrophage Colony Stimulating Factor Aliases: CSF1; CSF-1 Entrez Gene IDs: 1435 (Human); 12977 (Mouse) Background: M-CSF/CSF-1 M-CSF, also known as CSF-1, is a four-alpha-helical-bundle cytokine that is the primary regulator of macrophage survival, proliferation and differentiation. M-CSF is also essential for the survival and proliferation of osteoclast progenitors. M-CSF also primes and enhances macrophage killing of tumor cells and microorganisms, regulates the release of cytokines and other inflammatory modulators from macrophages, and stimulates pinocytosis. M-CSF increases during pregnancy to support implantation and growth of the decidua and placenta. Sources of M-CSF include fibroblasts, activated macrophages, endometrial secretory epithelium, bone marrow stromal cells and activated endothelial cells. The M-CSF receptor (c-fms) transduces its pleotropic effects and mediates its endocytosis. M-CSF mRNAs of various sizes occur. Full length human M-CSF transcripts encode a 522 amino acid (aa) type I transmembrane (TM) protein with a 464 aa extracellular region, a 21 aa TM domain, and a 37 aa cytoplasmic tail that forms a 140 kDa covalent dimer. Differential processing produces two proteolytically cleaved, secreted dimers. One is an N- and O- glycosylated 86 kDa dimer, while the other is modified by both glycosylation and chondroitin-sulfate proteoglycan (PG) to generate a 200 kDa subunit. Although PG-modified M-CSF can circulate, it may be immobilized by attachment to type V collagen. Shorter transcripts encode M-CSF that lack cleavage and PG sites and produce an N-glycosylated 68 kDa TM dimer and a slowly produced 44 kDa secreted dimer. Although forms may vary in activity and half-life, all contain the N-terminal 150 aa portion that is necessary and sufficient for interaction with the M-CSF receptor. The first 223 aa of mature human M-CSF shares 88%, 86%, 81% and 74% aa identity with corresponding regions of dog, cow, mouse and rat M-CSF, respectively. Human M-CSF is active in the mouse, but mouse M-CSF is reported to be species-specific.