>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.10 EU per 1 μg of the protein by the LAL method.
14.7 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
GM-CSF was initially characterized as a factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It is also a growth factor for erythroid, megakaryocyte, and eosinophil progenitors. GM-CSF is produced by a number of different cell types (including T cells, B cells, macrophages, mast cells, endothelial cells, fibroblasts, and adipocytes) in response to cytokine or inflammatory stimuli. On mature hematopoietic cells, GM-CSF is a survival factor for and activates the effector functions of granulocytes, monocytes/macrophages, and eosinophils (1, 2). GM-CSF promotes a Th1 biased immune response, angiogenesis, allergic inflammation, and the development of autoimmunity (3 - 5). It shows clinical effectiveness in ameliorating chemotherapy-induced neutropenia, and GM-CSF transfected tumor cells are utilized as cancer vaccines (6, 7). The 22 kDa glycosylated GM-CSF, similar to IL‑3 and IL‑5, is a cytokine with a core of four bundled alpha ‑helices (8 - 10). Mature rat GM-CSF shares 56% ‑ 69% amino acid sequence identity with canine, feline, human, mouse, and porcine GM‑CSF. GM‑CSF exerts its biological effects through a heterodimeric receptor complex composed of GM‑CSF R alpha /CD116 and the signal transducing common beta chain (CD131) which is also a component of the high-affinity receptors for IL-3 and IL-5 (11, 12). In addition, GM-CSF binds a naturally occurring soluble form of GM‑CSF R alpha (13). Rat GM‑CSF is active on mouse cells, although mouse GM‑CSF is only weakly active on rat cells (14, 15).
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