>95%, by SDS-PAGE with silver staining, under reducing conditions.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When
Human Fibronectin Fragment 4 (Catalog # 3624-FN)
is immubilized at 1 μg/mL, 100 μL/well, Recombinant Human MIA
binds with a typical ED50 of 1-6 μg/mL.
E. coli-derived Gly25-Gln131, with an N-terminal Met
When Recombinant Human Fibronectin Fragment 4(Catalog # 3624-FN) is coated at 1 μg/mL, Recombinant Human MIA (Catalog # 9250-IA) binds with atypical ED50 of 1-6 μg/mL.
Melanoma Inhibiting Activity (MIA), also known as cartilage-derived retinoic acid-sensitive protein (CD-RAP), is an approximately 11-15 kDa protein that is secreted as a noncovalent homodimer and is structurally related to OTOR/Otoraplin and MIA-2 (1). Mature human MIA contains a SH3 domain and shares 90% and 92% amino acid sequence identity with mouse and rat MIA, respectively (2). Alternative splicing generates a short isoform that lacks the SH3 domain (3). MIA is widely expressed in developing and regenerating cartilage and in the endothelium and parenchyma of developing lungs (4). MIA disrupts cellular interactions with the extracellular matrix by binding to Integrins alpha 4 beta 1 and alpha 5 beta 1 (5). It competes with Fibronectin fragments for Integrin binding and interferes with Integrin signaling (5). It also functions as a chemoattractant for mesenchymal stem cells and enhances their BMP-2 and TGF-beta 3 induced differentiation into chondrocytes [tscheud]. MIA-deficient mice exhibit delayed chondrocyte differentiation but enhanced chondrocyte proliferation and cartilage repair (7). MIA is up-regulated in several cancers including malignant melanoma, lung adenoma, metastatic oral squamous cell carcinoma, neurofibromatosis type 1 (NF-1)-related tumors, and pancreatic cancer (2, 4, 8-10). It is selectively secreted and internalized from the trailing pole of migrating cells (11, 12). This polarization reduces cellular attachment to the matrix at the trailing pole and contributes to directional tumor cell migration (2, 10, 13, 14).
Schmidt, J. et al. (2013) Histol. Histopathol. 28:421.
Blesch, A. et al. (1994) Cancer Res. 54:5695.
Hau, P. et al. (2002) J. Invest. Dermatol. 119:562.
Lin, S. et al. (2008) Dev. Biol. 316:441.
Bauer, R. et al. (2006) J. Biol. Chem. 281:11669.
Tscheudschilsuren, G. et al. (2006) Exp. Cell Res. 312:63.
Schmid, R. et al. (2010) Cell Death Dis. 1:e97.
Marr, D.G. et al. (2004) Int. J. Oncol. 25:105.
Sasahira, T. et al. (2010) Eur. J. Cancer 46:2285.
El Fitori, J. et al. (2005) Cancer Cell Int. 5:3.
Schmidt, J. et al. (2010) Cell Res. 20:1224.
Schmidt, J. and A.K. Bosserhoff (2009) Int. J. Cancer 125:1587.