Recombinant Mouse DMP-1 Protein, CF Summary
Product Specifications
Leu17-Tyr503, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
4386-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.
|
Reconstitution Calculator
Background: 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.
- Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
- MacDougall, M. et al. (1998) J. Bone Miner. Res. 13:422.
- 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.
Citations for Recombinant Mouse 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
Filter your results:
Filter by:
-
Self-assembly peptide P11-4 induces mineralization and cell-migration of odontoblast-like cells
Authors: IJS Araújo, GN Guimarães, RA Machado, LE Bertassoni, RPW Davies, RM Puppin-Ron
Journal of dentistry, 2022-04-21;121(0):104111.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Bone formation regulates circulating concentrations of fibroblast growth factor 23.
Authors: Samadfam R, Richard C, Nguyen-Yamamoto L, Bolivar I, Goltzman D
Endocrinology, 2009-10-09;150(11):4835-45.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Mouse DMP-1 Protein, CF
There are currently no reviews for this product. Be the first to review Recombinant Mouse DMP-1 Protein, CF and earn rewards!
Have you used Recombinant Mouse DMP-1 Protein, CF?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image