Recombinant Human CREG Protein Summary
Product Specifications
Met1-Gln220, 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.
2380-CR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
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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2380-CR/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 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.
|
Reconstitution Calculator
Background: CREG
Cellular repressor of E1A-stimulated genes (CREG) is a 25 - 35 kDa member of the CREG family of proteins. It is a secreted glycoprotein ubiquitously expressed in mammals. Human CREG is synthesized as a 220 amino acid (aa) precursor that contains a 31 aa signal sequence and a 189 aa mature chain. The mature chain contains three potential sites for N-linked glycosylation. Human CREG shares 78% aa sequence identity with mouse CREG (1, 2, 3). It antagonizes 12SE1A-mediated transcriptional activation of both adenovirus E2 and cellular heat shock protein 70 promoters (1, 3). Studies show that it inhibits E1A-mediated transformation of primary cultured rat kidney cells and promotes human embryonic carcinoma cell (NTERA-2) differentiation (1, 4). Other studies show that following forced over-expression in the medium of NTERA-2 cells, CREG inhibits cell cycle progression and induces cellular differentiation even in the absence of an inducer such as retinoic acid (1, 5).
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 (1). 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 (1). Moreover, CREG is down-regulated in the vascular media after balloon injury to the rabbit carotid artery (1). Adenovirus-mediated CREG over-expression in injured arteries inhibits SMCs proliferation and attenuates neointimal hyperplasia in vivo (1, 6). 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 (1).
Of the several proteins that have been reported to interact with CREG, the cation-independent mannose-6-phosphate (M6P)/ insulin-like growth factor II receptor (IGF2R) has been shown to be required for its growth-suppressive activity (1, 6). Researchers' findings indicate that CREG protein may be a target for cell growth inhibition mediated by attenuation of IGF-II-induced endocytosis of its membrane receptor M6P/IGF2R (1). Delivering recombinant CREG protein in vivo may provide therapeutic benefits for some pathological proliferative diseases, such as arterial restenosis after angioplasty, atherosclerosis, and human cancers (1).
- Han, Y-L. et al. (2008) Genes Cells 13:977.
- Han, Y. et al. (2008) Cardiovasc. Res. 78:597.
- Veal, E. et al. (1998) Mol. Cell. Biol. 18:5032.
- Veal, E. et al. (2000) Mol. Cell. Biol. 19:2120.
- DiBacco, A. and G. Gill (2003) Oncogene 22:5436.
- Wang, N. et al. (2008) Scand. J. Immunol. 67:340.
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