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Recombinant Rat RAGE Fc Chimera Protein, CF

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Product Details

Summary
Reactivity RtSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Rat RAGE Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. rrRAGE/Fc Chimera immobilized at 5 µg/mL (100 µL/well) on a goat anti-human IgG Fc antibody-coated plate (0.5 µg/well) can bind biotinylated advanced glycation endproducts of bovine serum albumin (AGE-BSA, Catalog # BT4127) with a linear range of 0.02-15 µg/mL.
Source
Mouse myeloma cell line, NS0-derived rat RAGE protein
Rat RAGE
(Gln24 - Ala342)
Accession # Q63495		 IEGRMD Human IgG1
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained: Gln24 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Ager
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
60 kDa (monomer).
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
80-90 kDa, reducing conditions
Publications
Read Publication using 1616-RG.

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
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Rat RAGE Fc Chimera Protein, CF

  • advanced glycosylation end product-specific receptor
  • AGER
  • RAGE isoform delta
  • RAGE isoform sRAGE-delta
  • RAGE
  • Receptor for advanced glycosylation end products
  • receptor for advanced glycosylation end-products
  • SCARJ1

Background

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 rat RAGE consists of a 319 amino acid (aa) extracellular domain (ECD) with one Ig-like V-type domain and two Ig-like C-type domains, a 21 aa transmembrane segment, and a 40 aa cytoplasmic domain (10). Within the ECD, rat RAGE shares 79% and 91% aa sequence identity with human and mouse RAGE, respectively. 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).
  1. Schleicher, E. and U. Friess (2007) Kidney Int. Suppl. 106:S17.
  2. Herold, K. et al. (2007) J. Leukoc. Biol. 82:204.
  3. Thornalley, P.J. (2006) J. Ren. Nutr. 16:178.
  4. Goldin, A. et al. (2006) Circulation 114:597.
  5. Ramasamy, R. et al. (2005) Glycobiology 15:16R.
  6. Kislinger, T. et al. (1999) J. Biol. Chem. 274:31740.
  7. Yan, S.D. et al. (1996) Nature 382:685.
  8. Huttenen, H. et al. (2000) J. Biol. Chem. 275:40096.
  9. Chavakis, T. et al. (2003) J. Exp. Med. 198:1507.
  10. Renard, C. et al. (1997) Mol. Pharmacol. 52:54.
  11. Yonekura H, et al. (2003) Biochem. J. 370:1097.
  12. Koyama, H. et al. (2007) Mol. Med. 13:625.
  13. Hori, O. et al. (1995) J. Biol. Chem. 270:25752.
  14. Brett, J. et al. (1993) Am. J. Pathol. 143:1699.
  15. Bierhaus, A. et al. (2006) Curr. Opin. Investig. Drugs 7:985.

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Publications for AGER (1616-RG)(1)

We have publications tested in 1 application: ELISA (Standard).


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Bioinformatics

Gene Symbol Ager
Uniprot