Recombinant Mouse MEPE/OF45 Protein, CF Summary
Details of Functionality |
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. |
Source |
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 |
Ser147 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Mepe |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
31.6 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
40-55 kDa, reducing conditions |
Packaging, Storage & Formulations
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 400 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse MEPE/OF45 Protein, CF
Background
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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