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Recombinant Human DMP-1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Human DMP-1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rhIntegrin alpha v beta 3 at 2 µg/mL can bind rhDMP-1 with an apparent
KD <20 nM.
Source
Mouse myeloma cell line, NS0-derived human DMP-1 protein
Leu17-Tyr497 & Asp202-Tyr497, both with a C-terminal 6-His tag & Leu17-Ser201
Accession #
N-terminal Sequence
Leu17 & Asp202
Protein/Peptide Type
Recombinant Proteins
Gene
DMP1
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
53.1 kDa, 19.7 kDa and 33.4 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
20-90 kDa, reducing conditions
Publications
Read Publications using
4129-DM in the following applications:

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.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human DMP-1 Protein, CF

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

Background

Dentin matrix protein 1 (DMP-1) is a member of the SIBLING family that also includes bone sialoprotein, dentin sialophosphoprotein, MEPE, and osteopontin. These highly phosphorylated integrin-binding proteins are rich in acidic amino acids and function in the formation of calcified bone and tooth matrix (1, 2). The 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). Rodent DMP-1 is cleaved by BMP-1 family proteases at a single site which is conserved in human, generating a 37 kDa N-terminal and a 57 kDa C-terminal 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 targeted to the nucleus, where 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 tethering of MMP-9 to the cell surface via CD44 and integrins alpha v beta 3 and alpha v beta 5 promotes 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 human DMP-1 shares 61% - 67% amino acid sequence identity with bovine, mouse, and rat DMP-1.

  1. Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
  2. Hirst, K.L. et al. (1997) Genomics 42:38.
  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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Bioinformatics

Gene Symbol DMP1
Uniprot