CREG, Recombinant, Mouse (Cellular Repressor of E1A-stimulated Genes 1, CREG 1, CREG, Protein CREG1)

Cellular repressor of E1A-stimulated genes (CREG) is a 28-33kD member of the CREG family of proteins. Mouse CREG is synthesized as a 220aa precursor that contains a 31 aa signal sequence and a 189 aa mature chain (SwissProt # O88668) (1, 2). Mass spectrometric analysis of recombinant CREG revealed that the protein contains phosphorylated oligosaccharides at either of its two N-glycosylation sites (1). Mouse CREG shares 78% aa sequence identity with human CREG. CREG is a secreted glycoprotein ubiquitously expressed in mammals (3). It is largely secreted by fibroblasts missing both mannose 6-phosphate receptors (1). This is not observed in cells lacking only one of them (1). CREG is proposed to participate in a wide range of cellular processes. Among them, CREG has been found to antagonize transcriptional and cellular transformation by the adenoviral E1A oncoprotein (1, 3, 4), to induce differentiation while attenuating cellular proliferation (1, 3, 4, 5), to regulate the levels of the signaling kinases ERK1/2 (1, 6), and to mediate the glucocorticoid-induced proliferation of ileal epithelial cells (1, 7). These observations have led to the notion that CREG may play an important role in the control of cell growth and differentiation (1, 3). In a search for potential interaction partners, CREG was found to bind directly to the mannose 6-phosphate/insulin-like growth factor II receptor (M6P/IGF2R) (1). Since this interaction was shown to depend on N-glycosylation of CREG, it was inferred that CREG binds to M6P/IGF2R via M6P residues located in its N-glycans (1, 3, 8). Other studies have shown that CREG interacts with M6P/IGF2R in an M6P-dependent manner (1, 9-12). Recent results indicate that human CREG carries M6P moieties at two of its three N-glycosylation sites (1, 13). Han et al. showed that CREG is significantly up-regulated at both the mRNA and protein levels during phenotypic conversion of proliferative and synthetic smooth muscle cells (SMCs) to non-proliferative and differentiated SMCs in vitro (3). In addition, CREG over-expression in cultured SMCs may inhibit cellular proliferation and promote differentiation; whereas CREG knockdown prevents serum starvation-induced SMCs maturation and growth arrest (3). Moreover, CREG is down-regulated in the vascular media after balloon injury in the rabbit carotid artery (3). Adenovirus-mediated CREG over-expression in injured arteries inhibits SMCs proliferation and attenuates neointimal hyperplasia in vivo (3, 14). Research thus suggests that CREG plays a critical role in keeping cell or tissue in a mature, homeostatic state by antagonizing pathological de-differentiation and overgrowth (3).\n\nSource:\nRecombinant corresponding to aa32-220 of mouse CREG, fused with 6-His tag at C-terminal, expressed in mouse myeloma cell line, NS0.\n\nMolecular Weight: \n~22.3kD\n\nEndotoxin Level:\n(same/less than)1EU/1ug (LAL)\n\nBiological Activity:\nMeasured by its binding ability in a functional ELISA. When recombinant human IGF-II R is immobilized at 2ug/ml (100ul/well), the concentration of recombinant mouse CREG that produces 50% of the optimal binding response is found to be ~3-15ng/ml.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with PBS. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Prices direct from United States Biological

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

C7918-70C

Size

25ug

Form

Supplied as a lyophilized powder in PBS, BSA. Reconstitute with PBS, 0.1% human or bovine serum albumin to 100ug/ml.

Purity

~95% (SDS-PAGE)

References

1. Schahs, P. et al. (2008) Exp. Cell Res. 314:3036. 2. Han, Y. et al. (2008) Cardiovasc. Res. 78:597. 3. Han, Y-L. et al. (2008) Genes Cells 13:977. 4. Veal, E. et al. (1998) Mol. Cell. Biol. 18:5032.5. Veal, E. et al. (2000) Oncogene 19:2120. 6. Xu, L. et al. (2004) J. Hypertens. 22:1579. 7. Gordon, P.V. et al. (2005) J. Endocrinol. 185:265. 8. Di Bacco, A. et al. (2003) Oncogene 22:5436. 9. Journet, A. et al. (2000) Electrophoresis 21:3411. 10. Journet, A. et al. (2002) Proteomics 2:1026. 11. Sleat, D.E. et al. (2005) Proteomics 5:1520. 12. Kollmann, K. et al. (2005) Proteomics 5:3966. 13. Sleat, D.E. et al. (2006) Mol. Cell. Proteomics 5:686. 14. Wang, N. et al. (2008) Scand. J. Immunol. 67:340.