Recombinant Human MIA Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When
Recombinant
Human Fibronectin Fragment 4 (Catalog # 3624-FN)
is immubilized at 1 μg/mL, 100 μL/well, Recombinant Human MIA
binds with a typical ED 50 of 1-6 μg/mL. |
Source |
E. coli-derived human MIA protein Gly25-Gln131, with an N-terminal Met |
Accession # |
|
N-terminal Sequence |
Met, Gly25 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE with silver staining, under reducing conditions. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
12 kDa. 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 |
10 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS and Trehalose. |
Purity |
>95%, by SDS-PAGE with silver staining, under reducing conditions. |
Reconstitution Instructions |
Reconstitute at 400 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human MIA Protein, CF
Background
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.
- Poser, I. et al. (2004) Oncogene 23:6115.
- Guba, M. et al. (2000) Brit. J. Cancer 83:1216.
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