Recombinant Mouse MEPE/OF45 Protein, CF Summary
Product Specifications
The ED50 for this effect is 0.1-0.4 μg/mL.
Optimal dilutions should be determined by each laboratory for each application.
Met1-Asp433, with a C-terminal 10-His tag
Insertion: Ala199-Val-Gly200 & Lys310-Gly-Gly311
Substitution: Leu164Phe, Pro182Ser, His189Gln, Arg209His, Leu211Val, Ile220Val, Met224Thr, Ser225Asn, Gly258Glu, Asn285Asp, Val313Gly, Pro325Leu, Ser332Ala, Arg351Lys, Ser402Leu & Asn406His
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.
6150-ME
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 400 μg/mL in 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.
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Reconstitution Calculator
Background: MEPE/OF45
MEPE (matrix extracellular phosphoglycoprotein), known as OF45 in mouse and rat, is a 55 kDa member of the SIBLING protein family. MEPE is primarily expressed in bone and dentin, where it regulates the mineralization of those tissues (1 - 3). The mouse MEPE cDNA encodes a 441 amino acid (aa) precursor that includes a 16 aa signal sequence (4), and shares 45% homology with the human MEPE. MEPE contains multiple consensus sites for post-translational modifications, including N-linked glycosylation, N-myristoylation, glycosaminoglycan attachment, and phosphorylation by a variety of kinases. MEPE also contains several putative proteolytic cleavage sites and one integrin-binding RGD motif (3 - 5). There is therefore considerable potential for post-translational regulation of MEPE function and its degradation products. MEPE is secreted by osteoblasts and dental pulp stem cells during the mineralization process (6 - 8) and also by nonmineralizing tissues including epithelial cells in the renal proximal tubule and salivary duct (9, 10). MEPE has an inhibitory function in bone formation (6), although a peptide corresponding to aa 242 - 264 stimulates new bone formation and the proliferation of osteoblasts and dental pulp stem cells (11, 12). MEPE contains one C-terminal ASARM motif common to SIBLING proteins. Similar to intact MEPE, the ASARM peptide inhibits bone mineralization and plays a central role in the phosphaturia and reduced mineralization of X-linked hypophosphatemic rickets (HYP) and tumor-induced osteomalacia (TIO) (13, 14). The zinc metalloprotease Phex binds directly to MEPE via the ASARM motif and prevents ASARM cleavage (14, 15). Multiple inactivating mutations in Phex are found in HYP and TIO and result in the increased liberation of ASARM peptide (16). Both MEPE and ASARM peptide are elevated in these disorders of mineralization and phosphate metabolism (13).
- Fisher, L.W. and N.S. Fedarko (2003) Connect. Tiss. Res. 44:33.
- Quarles, L.D. (2003) Am. J. Physiol. 285:E1.
- Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
- Argiro, L. et al. (2001) Genomics 74:342.
- Rowe, P.S.N. et al. (2000) Genomics 67:54.
- Gowen, L.C. et al. (2003) J. Biol. Chem. 278:1998.
- Siggelkow, H. et al. (2004) Bone 35:570.
- Liu, H. et al. (2005) Arch. Oral Biol. 50:923.
- Ogbureke, K.U.E. and Fisher, L.W. (2005) Kidney Int. 68:155.
- Ogbureke, K.U.E. and L.W. Fisher (2004) J. Dent. Res. 83:664.
- Hayashibara, T. et al. (2004) J. Bone Miner. Res. 19:455.
- Liu, H. et al. (2004) J. Dent. Res. 83:496.
- Bresler, D. et al. (2004) J. Endocrinol. 183:R1.
- Rowe, P.S.N. et al. (2005) Bone 36:33.
- Guo, R. et al. (2002) Biochem. Biophys. Res. Commun. 297:38.
- Rowe, P.S. (2004) Crit. Rev. Oral Biol. Med.15:264.
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