Measured by its ability to modulate collagen fibrillogenesis. 20 µg/mL of rmDermatopontin can significantly enhance the rate of collagen fibrillogenesis.
Source
Mouse myeloma cell line, NS0-derived mouse Dermatopontin protein Gln19-Val201 with a C-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
22.8 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
23 kDa, reducing conditions
Publications
Read Publication using 5749-DP in the following applications:
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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 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 Mouse Dermatopontin Protein, CF
Dermatopontin
DPT
Eq1
TRAMP
Tyrosine-rich acidic matrix protein
Background
Dermatopontin, also known as TRAMP (tyrosine rich acidic matrix protein) and EQ-1 (early quiescence-1), is a widely expressed noncollagenous protein component of the extracellular matrix (1, 2). Mature mouse Dermatopontin shares 92% and 97% amino acid sequence identity with human and rat Dermatopontin, respectively. It is a 22 kDa molecule that is tyrosine sulfated but not glycosylated (3, 4). Dermatopontin contains three disulfide bonded loop structures that enclose conserved hexapeptide motifs (5). It accelerates collagen fibril formation in vitro, and Dermatopontin deficient mice exhibit altered collagen matrix deposition and organization (6 - 8). Dermatopontin is downregulated in fibrotic growths such as leiomyoma and scar tissue (9, 10). It binds both TGF-beta and the proteoglycan Decorin, interactions that can increase the bioavailability of TGF-beta (11, 12). Dermatopontin promotes bone mineralization under the control of the vitamin D receptor and inhibits BMP-2 effects on osteoblast precursors (13, 14).
Okamoto, O. and S. Fujiwara (2006) Connect. Tissue Res. 47:177.
Tzen, C.Y. and Y.W. Huang (2004) Exp. Cell Res. 294:30.
Forbes, E.G. et al. (1994) FEBS Lett. 351:433.
Cronshaw, A.D. et al. (1993) Matrix 13:255.
Neame, P.J. et al. (1989) J. Biol. Chem. 264:5474.
MacBeath, J.R.E. et al. (1993) J. Biol. Chem. 268:19826.
Takeda, U. et al. (2002) J. Invest. Dermatol. 119:678.
Cooper, L.J. et al. (2006) Invest. Opthalmol. Vis. Sci. 47:3303.
Catherino, W.H. et al. (2004) Genes Chromosomes Cancer 40:204.
Kuroda, K. et al. (1999) J. Invest. Dermatol. 112:706.
Okamoto, O. et al. (1996) J. Biochem. 119:106.
Okamoto, O. et al. (1999) Biochem. J. 337:537.
Pochampally, R.R. et al. (2007) J. Bone Miner. Res. 22:1338.
Behnam, K. et al. (2006) Connect. Tissue Res. 47:271.
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