Dentin Matrix Protein 1, Recombinant, Mouse (DMP1)

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 37kD N-terminal (aa 17-212) and a 57kD 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 aVb3 and aVb5, 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 aVb3, 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.\n\nA DNA sequence encoding the mature mouse DMP-1 (Leu 17-Tyr 503; Accession # AAI13754) fused with 6X Histidines at the C-terminus was expressed in a mouse myeloma cell line, NS0.\n\nCalculated molecular mass of 52.9kD. The recombinant protein migrates anomalously in SDS-PAGE under reducing conditions as a 57kD monomer, a non-disulfide linked dimer of 99kD, and a tetramer of 180kD.\n\nActivity: Measured by its ability to bind rhIntegrin aVb3.\n\nStorage and Stability:\nLyophilized powder may be stored at 4 degrees C for short-term only. Reconstitute to nominal volume by adding sterile PBS and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

D3154-75

Size

50ug

Form

Supplied as a lyophilized powder in PBS. Reconstitute with PBS to (same/more than)100ug/ml.

Purity

(same/more than) 85%, as determined by SDS-PAGE under reducing conditions and visualized by silver stain.\nEndotoxin: (same/less than) 1EU/1ug.

References

1. Qin, C. et al., 2004, Crit. Rev. Oral Biol. Med. 15:126. 9. Narayanan, K. et al., 2003, J. Biol. Chem. 278:17500.\n2. MacDougall, M. et al., 1998, J. Bone Miner. Res. 13:422. 10. Narayanan, K. et al., 2006, J. Biol. Chem. 281:19064.\n3. He, G. et al., 2003, Nat. Mater. 2:552. 11. Lorenz-Depiereux, B., et al., 2006, Nat. Genet. 38:1248.\n4. Gajjeraman, S. et al., 2007, J. Biol. Chem. 282:1193. 12. Feng, J.Q. et al., 2006, Nat. Genet. 38:1310.\n5. He, G. et al., 2005, Biochemistry 44:16140. 13. Fedarko, N.S. et al., 2004, FASEB J. 18:735.\n6. Steiglitz, B.M. et al., 2004, J. Biol. Chem. 279:980. 14. Karadag, A. et al., 2005, Cancer Res. 65:11545.\n7. Qin, C. et al., 2006, J. Biol. Chem. 281:8034. 15. Jain, A. et al., 2002, J. Biol. Chem. 277:13700.\n8. Lu, Y. et al., 2007, Dev. Biol. 303:191.