Recombinant Mouse DMP-1 Protein, CF


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Product Details

Reactivity MuSpecies Glossary
Applications Binding Activity

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Recombinant Mouse DMP-1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhIntegrin  alpha V beta 3 at 5 µg/mL can bind rmDMP-1 with an apparent KD < 25 nM.
Mouse myeloma cell line, NS0-derived mouse DMP-1 protein
Leu17-Tyr503, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>85%, 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.


Theoretical MW
52.9 kDa (monomer).
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.
57 kDa, 99 kDa and 180 kDa, reducing conditions
Read Publication using
4386-DM 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.
>85%, by SDS-PAGE under reducing conditions and visualized by silver stain
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 Mouse DMP-1 Protein, CF

  • ARHP
  • ARHR
  • dentin matrix acidic phosphoprotein 1
  • dentin matrix acidic phosphoprotein
  • Dentin matrix protein 1
  • DMP1
  • DMP-1


Dentin matrix protein 1 (DMP-1) is a member of the SIBLING family of proteins that includes bone sialoprotein, dentin sialophosphoprotein, MEPE, and osteopontin. These are highly phosphorylated integrin-binding proteins that are rich in acidic amino acids and function in the formation of calcified bone and tooth matrix (1, 2). Its phosphate content, spacing of acidic residues, and calcium-dependent dimerization of DMP-1 contribute to its ability to sequester calcium phosphate clusters and promote hydroxyapatite (HA) crystal formation (3 - 5). Mature mouse DMP-1 is 487 amino acids (aa) in length. It contains a poly-Pro segment (aa 41 - 44) and an RGD binding motif (aa 350 - 352). DMP-1 may be cleaved by BMP-1 family proteases at a single site which is conserved in human, generating a 37 kDa N-terminal (aa 17 - 212) and a 57 kDa C-terminal (aa 213 - 503) fragment (6). The N-terminal fragment in rat carries chondroitin sulfate (7). The C-terminal fragment alone can nucleate HA crystals, while crystal growth into a needle-like morphology is inhibited by the N-terminal fragment (3, 4). Crystal maturation is dependent on the presence of type I collagen (4). DMP-1 is required for odontoblast differentiation as well as dentin formation (8). Nonphosphorylated DMP-1 is retained intracellularly where it is targeted to the nucleus. Here, it activates the transcription of odontoblast and osteoblast specific genes (9, 10). Early in osteoblast maturation, nuclear DMP-1 is extensively phosphorylated by casein kinase II, triggering its secretion (9). DMP-1 mutations in humans are associated with hypophosphatemia and FGF23 overexpression (11, 12). DMP-1 induces the activation of proMMP-9 and displaces mature MMP-9 from TIMP1 (13). DMP-1 tethers MMP-9 to the cell surface via CD44 and integrins alpha V beta 3 and alpha V beta 5, promoting tumor cell invasiveness in vitro (14). Full length DMP-1 circulates in human serum in a tight complex with complement factor H (13, 14). When first bound to CD44 or integrin alpha V beta 3, DMP-1 can anchor factor H to the cell surface and protect the cell from complement-mediated lysis (15). Mature mouse DMP-1 shares 63%, 61%, and 87% aa sequence identity with bovine, human, and rat DMP-1, respectively.

  1. Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126. 
  2. MacDougall, M. et al. (1998) J. Bone Miner. Res. 13:422. 
  3. He, G. et al. (2003) Nat. Mater. 2:552. 
  4. Gajjeraman, S. et al. (2007) J. Biol. Chem. 282:1193. 
  5. He, G. et al. (2005) Biochemistry 44:16140. 
  6. Steiglitz, B.M. et al. (2004) J. Biol. Chem. 279:980. 
  7. Qin, C. et al. (2006) J. Biol. Chem. 281:8034. 
  8. Lu, Y. et al. (2007) Dev. Biol. 303:191.
  9. Narayanan, K. et al. (2003) J. Biol. Chem. 278:17500.
  10. Narayanan, K. et al. (2006) J. Biol. Chem. 281:19064.
  11. Lorenz-Depiereux, B. et al. (2006) Nat. Genet. 38:1248.
  12. Feng, J.Q. et al. (2006) Nat. Genet. 38:1310.
  13. Fedarko, N.S. et al. (2004) FASEB J. 18:735.
  14. Karadag, A. et al. (2005) Cancer Res. 65:11545.
  15. Jain, A. et al. (2002) J. Biol. Chem. 277:13700.

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Publications for DMP-1 (4386-DM)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Bioassay.

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Gene Symbol Dmp1