Recombinant Canine RAGE Protein, CF Summary
Product Specifications
Asp25-Val339, 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.
4750-RG
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile 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: RAGE/AGER
Advanced glycation endproducts (AGEs) are adducts formed by the non-enzymatic glycation of macromolecules. AGE formation is accelerated in oxidative and hyperglycemic conditions, diabetes, renal failure, atherosclerosis, Alzheimer’s disease, arthritis, and in normal aging (1 - 5). Receptor for advanced glycation endproducts (RAGE) is a 35 kDa type I transmembrane protein belonging the immunoglobulin superfamily. Besides AGEs, RAGE binds beta -amyloid peptide, S100/calgranulin family proteins, HMGB1/amphoterin, and leukocyte integrins (6 - 9). Mature canine RAGE consists of a 383 amino acid (aa) extracellular domain (ECD) with one Ig-like V-type domain and two Ig-like C-type domains, a 23 aa transmembrane segment, and a 43 aa cytoplasmic domain (10). Within the ECD, canine RAGE shares 73% - 77% aa sequence identity with human, mouse, and rat RAGE. In human, soluble forms of RAGE are generated by alternate splicing and are associated with multiple disease states (11, 12). RAGE is expressed in the embryonic central nervous system and on macrophages, monocytes, smooth muscle cells, and endothelial cells (13 - 15). It is upregulated in response to AGE accumulation, and its activation induces a broad proinflammatory response (6, 15). The increased production of reactive oxygen species during inflammation promotes additional AGE formation and RAGE upregulation, a cycle that exacerbates diabetic complications and inflammation-induced tissue injury (2, 4).
- Schleicher, E. and U. Friess (2007) Kidney Int. Suppl. 106:S17.
- Herold, K. et al. (2007) J. Leukoc. Biol. 82:204.
- Thornalley, P.J. (2006) J. Ren. Nutr. 16:178.
- Goldin, A. et al. (2006) Circulation 114:597.
- Ramasamy, R. et al. (2005) Glycobiology 15:16R.
- Kislinger, T. et al. (1999) J. Biol. Chem. 274:31740.
- Yan, S.D. et al. (1996) Nature 382:685.
- Huttenen, H. et al. (2000) J. Biol. Chem. 275:40096.
- Chavakis, T. et al. (2003) J. Exp. Med. 198:1507.
- Murua Escobar, H. et al. (2006) Gene 369:45.
- Yonekura H, et al. (2003) Biochem. J. 370:1097.
- Koyama, H. et al. (2007) Mol. Med. 13:625.
- Hori, O. et al. (1995) J. Biol. Chem. 270:25752.
- Brett, J. et al. (1993) Am. J. Pathol. 143:1699.
- Bierhaus, A. et al. (2006) Curr. Opin. Investig. Drugs 7:985.
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