Recombinant Mouse MEPE/OF45 Protein, CF

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Recombinant Mouse MEPE/OF45 Protein, CF Summary

Product Specifications

>95%, 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.
Measured by its ability to induce adhesion of ATDC5 mouse chondrogenic cells.

The ED50 for this effect is 0.1-0.4 μg/mL.

Optimal dilutions should be determined by each laboratory for each application.

Mouse myeloma cell line, NS0-derived mouse MEPE/OF45 protein
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

Accession #
N-terminal Sequence
Predicted Molecular Mass
31.6 kDa
40-55 kDa, reducing conditions

Product Datasheets

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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.


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.
  • 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: 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).

  1. Fisher, L.W. and N.S. Fedarko (2003) Connect. Tiss. Res. 44:33.
  2. Quarles, L.D. (2003) Am. J. Physiol. 285:E1.
  3. Qin, C. et al. (2004) Crit. Rev. Oral Biol. Med. 15:126.
  4. Argiro, L. et al. (2001) Genomics 74:342.
  5. Rowe, P.S.N. et al. (2000) Genomics 67:54.
  6. Gowen, L.C. et al. (2003) J. Biol. Chem. 278:1998.
  7. Siggelkow, H. et al. (2004) Bone 35:570.
  8. Liu, H. et al. (2005) Arch. Oral Biol. 50:923.
  9. Ogbureke, K.U.E. and Fisher, L.W. (2005) Kidney Int. 68:155.
  10. Ogbureke, K.U.E. and L.W. Fisher (2004) J. Dent. Res. 83:664.
  11. Hayashibara, T. et al. (2004) J. Bone Miner. Res. 19:455.
  12. Liu, H. et al. (2004) J. Dent. Res. 83:496.
  13. Bresler, D. et al. (2004) J. Endocrinol. 183:R1.
  14. Rowe, P.S.N. et al. (2005) Bone 36:33.
  15. Guo, R. et al. (2002) Biochem. Biophys. Res. Commun. 297:38.
  16. Rowe, P.S. (2004) Crit. Rev. Oral Biol. Med.15:264.
Long Name
Matrix Extracellular Phosphoglycoprotein with ASARM Motif
Entrez Gene IDs
56955 (Human); 94111 (Mouse); 79110 (Rat)
Alternate Names
extracellular phosphoglycoprotein with ASARM motif (bone); matrix extracellular phosphoglycoprotein; MEPE; OF45; Osteoregulin


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