Measured by its ability to activate MSP R/Ron in MDA-MB-453 or T47D human breast cancer cells. 80 ng/mL of the recombinant human MSP significantly induces phosphorylation of MSP R/Ron measured by the Human Phospho-MSP R/Ron DuoSet® IC Kit (Catalog # DYC1947). Measured by its binding ability in a functional ELISA. When Recombinant Human MSPR/Ron Protein (Catalog #1947-MS) is represent at 100 ng/mL (100 µg/mL), The concentration of Recombinant Human MSP/MST1 that produces 50% optimal binding response is found to be 8-40 ng/mL.
Mouse myeloma cell line, NS0-derived human MSP/MST1 protein Gln19-Gly711
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<1.0 EU per 1 μg of the protein by the LAL method.
78.5 kDa (MSP alpha / beta ); 53.3 kDa ( alpha chain), 25.2 kDa ( beta chain). 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.
Macrophage stimulating protein (MSP), also known as HGF-like protein, and scatter factor-2, is a member of the HGF family of growth factors (1). MSP is secreted as an inactive single chain precursor (pro-MSP) that contains a PAN/APPLE-like domain, four kringle domains, and a peptidase S1 domain which lacks enzymatic activity (2). Human MSP shares 79% amino acid (aa) sequence identity with mouse MSP and 44% aa sequence identity with human HGF. Pro-MSP is secreted by hepatocytes under the positive and negative control of CBP in complex with either HNF-4 or RAR, respectively (3). Circulating pro-MSP is proteolytically cleaved in response to tissue injury to yield biologically active disulfide linked heterodimers consisting of a 45 - 62 kDa alpha and a 25 - 35 kDa beta chain (4, 5). Pro-MSP can be activated by MT-SP1, a transmembrane protease that is expressed on macrophages and is upregulated in many cancers (6). Heterodimeric MSP as well as the isolated beta chain bind to MSP R/Ron with high-affinity, although only heterodimeric MSP can induce receptor dimerization and signaling (7, 8). MSP induces macrophage and keratinocyte proliferation and osteoclast activation (9, 10). It also inhibits LPS- or IFN-induced iNOS and IL-12 expression by macrophages and prevents apoptosis of epithelial cells separated from the ECM (11, 12).
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