Human M-CSF Recombinant Protein Thermo Human M-CSF Recombinant Protein

2024-10-29

Human M-CSF Recombinant Protein

货号:PHC9504,PHC9501

规格:10μg,100μg

市场价格:3492,19964

产品类型:细胞因子添加物

品牌:Gibco

产品详细信息

•Purity: ≥95% by SDS-PAGE•Endotoxin Concentration: <0.1 ng/µg Activity: ED50 ≤5 ng/mL•Molecular Weight: 38 kDaReconstitution: Lyophilized human M-CSF should be reconstituted in 20mM Tris-HCl, pH 8.0 to a concentration of 0.1-1.0 mg/mL. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein, such as 0.1% BSA and store in working aliquots at -20°C to -80°C.Storage: Lyophilized human M-CSF should be stored at 2°C to 8°C, preferably desiccated. Store reconstituted human M-CSF at ≤-20°C (not in a frost-free freezer). Keep freeze-thaw cycles to a minimum.

靶标信息

M-CSF (Macrophage colony-stimulating factor, CSF-1) is a survival factor essential for the proliferation and development of monocytes, macrophages, and osteoclast progenitor cells. M-CSF also induces VEGF (vascular endothelial growth factor) secretion by macrophages, thereby mediating mobilization of endothelial progenitor cells and neovascularization. M-CSF is present as several bioactive isoforms that differ in potency and stability. The full-length protein is synthesized as a membrane-spanning protein that can be expressed on the cell surface or further cleaved and modified in the secretory vesicle. Further, M-CSF is a disulfide-bonded homodimer which is processed into one of two isoforms, a glycoprotein or a proteoglycan that has been modified by the addition of chondroitin sulfate to each subunit. Binding of M-CSF to its receptor, c-Fms (CSF-1R or CD115) induces dimerization of the receptor followed by internalization and degradation of the complex. Functionally, M-CSF is known to stimulate differentiation of hematopoietic stem cells to monocyte-macrophage cell populations in culture. M-CSF acts through the CSF receptor 1. Although human M-CSF shows activity on mouse cells, mouse CSF shows no activity on human cells.

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