Recombinant Human DMP-1 Protein, CF

Catalog # Availability Size / Price Qty
4129-DM-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (2)
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Recombinant Human DMP-1 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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
Analysis
Leu17 & Asp202
Predicted Molecular Mass
53.1 kDa, 19.7 kDa and 33.4 kDa
SDS-PAGE
20-90 kDa, reducing conditions

Product Datasheets

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4129-DM

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

4129-DM

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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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.

References
  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.
Long Name
Dentin Matrix Protein 1
Entrez Gene IDs
1758 (Human); 13406 (Mouse); 25312 (Rat)
Alternate Names
ARHP; ARHR; dentin matrix acidic phosphoprotein 1; dentin matrix acidic phosphoprotein; Dentin matrix protein 1; DMP1; DMP-1

Citations for Recombinant Human DMP-1 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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  1. A molecular interactome of the glioblastoma perivascular niche reveals integrin binding sialoprotein as a mediator of tumor cell migration
    Authors: Y Ghochani, SD Muthukrish, A Sohrabi, R Kawaguchi, MC Condro, S Bastola, F Gao, Y Qin, J Mottahedeh, ML Iruela-Ari, N Rao, DR Laks, LM Liau, GW Mathern, SA Goldman, ST Carmichael, I Nakano, G Coppola, SK Seidlits, HI Kornblum
    Cell Reports, 2022-10-18;41(3):111511.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Dentin matrix protein 1 induces membrane expression of VE-cadherin on endothelial cells and inhibits VEGF-induced angiogenesis by blocking VEGFR-2 phosphorylation.
    Authors: Pirotte S, Lamour V, Lambert V, Alvarez Gonzalez ML, Ormenese S, Noel A, Mottet D, Castronovo V, Bellahcene A
    Blood, 2010-12-29;117(8):2515-26.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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