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 DuoSetIC human phospho-MSP R/Ron 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.
Source
Mouse myeloma cell line, NS0-derived human MSP/MST1 protein Gln19-Gly711
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Bioactivity2
Theoretical MW
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.
SDS-PAGE
81 kDa, 62 kDa and 30 kDa, reducing conditions
Publications
Read Publications using 352-MS in the following applications:
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% 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).
Wang, M.-H. et al. (2002) Scand. J. Immunol. 56:545.
Han, S. et al. (1991) Biochemistry 30:9768.
Muraoka, R.S. et al. (1999) Endocrinology 140:187.
Wang, M.-H. et al. (1996) J. Clin. Invest. 97:720.
Nanney, L.B. et al. (1998) J. Invest. Dermatol. 111:573.
Bhatt, A.S. et al. (2007) Proc. Natl. Acad. Sci. 104:5771.
Wang, M.-H. et al. (1997) J. Biol. Chem. 272:16999.
Danilkovitch, A. et al. (1999) J. Biol. Chem. 274:29937.
Wang, M.-H. et al. (1996) Exp. Cell Res. 226:39.
Kurihara, N. et al. (1998) Exp. Hematol. 26:1080.
Morrison, A.C. et al. (2004) J. Immunol. 172:1825.
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