Human DMP-1 Biotinylated Antibody Summary
Leu17-Tyr497
Accession # NP_001073380
Applications
Human DMP-1 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: DMP-1
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.
- Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
- Hirst, K.L. et al. (1997) Genomics 42:38.
- He, G. et al. (2003) Nat. Mater. 2:552.
- Gajjeraman, S. et al. (2007) J. Biol. Chem. 282:1193.
- He, G. et al. (2005) Biochemistry 44:16140.
- Steiglitz, B.M. et al. (2004) J. Biol. Chem. 279:980.
- Qin, C. et al. (2006 J. Biol. Chem. 281:8034.
- Lu, Y. et al. (2007) Dev. Biol. 303:191.
- Narayanan, K. et al. (2003) J. Biol. Chem. 278:17500.
- Narayanan, K. et al. (2006) J. Biol. Chem. 281:19064.
- Lorenz-Depiereux, B. et al. (2006) Nat. Genet. 38:1248.
- Feng, J.Q. et al. (2006) Nat. Genet. 38:1310.
- Fedarko, N.S. et al. (2004) FASEB J. 18:735.
- Karadag, A. et al. (2005) Cancer Res. 65:11545.
- Jain, A. et al. (2002) J. Biol. Chem. 277:13700.
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