>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.01 EU per 1 μg of the protein by the LAL method.
14.5 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.
20-35 kDa, reducing conditions
Read Publication using 7954-GM in the following applications:
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 (8‑12). Mature human GM‑CSF shares 63%‑70% amino acid sequence identity with canine, feline, porcine, and rat GM‑CSF and 54% with mouse 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 (13, 14). In addition, GM‑CSF binds a naturally occurring soluble form of GM‑CSF R alpha (15). Human GM‑CSF is active on canine and feline cells but not on murine cells (16‑18).
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