• Predicted molecular weight: 26.0 kDa
• No endotoxins, TAGS, and carrier-free
• Naturally folded and post-translationally modified

IBI recombinant proteins are expressed in Pichia pastoris (yeast) system which provides many advantages over E. coli systems. Yeast systems promote proper protein folding and post-translational modifications for greater bio-activity. The recombinant proteins are endotoxin free and are purified without HIS-TAGS or any other TAG. IBI’s yeast expression system has proven to produce more active proteins that more closely resemble their host form.

Macrophage colony-stimulating factor (M-CSF), also known as CSF-1, is a hematopoietic growth factor that is involved in the proliferation, differentiation, and survival of monocytes, macrophages, and bone marrow progenitor cells. M-CSF enhances expression of differentiation antigens and stimulates chemotactic, phagocytic and the killing activities of monocytes. M-CSF also stimulates production of several cytokines, including GM- CSF, G-CSF and IL-6 by priming monocytes. It also stimulates production and secretion of IL-8 and reactive nitrogen intermediates. In addition to the stimulation of hematopoiesis, M-CSF also stimulates differentiation and proliferation of osteoclast progenitor cells and cytotrophoblasts.

The recombinant mouse protein M-CSF has a predicted molecular weight of 26.0 kDa.

All IBI recombinant proteins are lyophilized and shipped at room temperature without carrier protein. Proteins can be reconstituted in sterile PBS with at least 0.1% of carrier protein such as BSA or cell assay media.

The M-CSF mouse protein can be used in cell culture, as an M-CSF ELISA Standard, and as a Western Blot Control.

Country of Origin: USA