Recombinant Human Dermatopontin Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

Recombinant Human Dermatopontin Protein, CF Summary

Details of Functionality
Measured by its ability to modulate collagen fibrillogenesis. 20 µg/mL of rhDermatopontin can significantly enhance the rate collagen fibrillogenesis.
Mouse myeloma cell line, NS0-derived human Dermatopontin protein
Gln19-Val201, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln19 predicted
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • 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.
23 kDa, reducing conditions
Read Publications using
4629-DP in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Dermatopontin Protein, CF

  • Dermatopontin
  • DPT
  • Eq1
  • Tyrosine-rich acidic matrix protein


Dermatopontin, also known as TRAMP (tyrosine rich acidic matrix protein), is a widely expressed noncollagenous protein component of the extracellular matrix (1, 2). Mature human Dermatopontin shares 96%, 92%, and 92% amino acid sequence identity with bovine, mouse, 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 down-regulated 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).

  1. Okamoto, O. and S. Fujiwara (2006) Connect. Tissue Res. 47:177.
  2. Superti-Furga, A. et al. (1993) Genomics 17:463.
  3. Forbes, E.G. et al. (1994) FEBS Lett. 351:433.
  4. Cronshaw, A.D. et al. (1993) Matrix 13:255.
  5. Neame, P.J. et al. (1989) J. Biol. Chem. 264:5474.
  6. MacBeath, J.R.E. et al. (1993) J. Biol. Chem. 268:19826.
  7. Takeda, U. et al. (2002) J. Invest. Dermatol. 119:678.
  8. Cooper, L.J. et al. (2006) Invest. Opthalmol. Vis. Sci. 47:3303.
  9. Catherino, W.H. et al. (2004) Genes Chromosomes Cancer 40:204.
  10. Kuroda, K. et al. (1999) J. Invest. Dermatol. 112:706.
  11. Okamoto, O. et al. (1996) J. Biochem. 119:106.
  12. Okamoto, O. et al. (1999) Biochem. J. 337:537.
  13. Pochampally, R.R. et al. (2007) J. Bone Miner. Res. 22:1338.
  14. Behnam, K. et al. (2006) Connect. Tissue Res. 47:271.

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Gene Symbol DPT