Recombinant Human RAGE Fc Chimera Protein, CF

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Recombinant Human RAGE Fc Chimera Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. rhRAGE/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 0.02-1 µg/mL.
Mouse myeloma cell line, NS0-derived human RAGE protein
Human RAGE
(Gln24 - Ala344)
Accession # Q15109
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
No results obtained: Gln24 predicted
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
61 kDa (monomer)
80-90 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.


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.
  • 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.
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Background: RAGE/AGER

Advanced glycation endproducts (AGE) are adducts formed by the non-enzymatic glycation or oxidation of macromolecules (1). AGE forms during aging and its formation is accelerated under pathophysiologic states such as diabetes, Alzheimer’s disease, renal failure and immune/inflammatory disorders. Receptor for Advanced Glycation Endoproducts (RAGE), named for its ability to bind AGE, is a multi-ligand receptor belonging the immunoglobulin (Ig) superfamily. Besides AGE, RAGE binds amyloid beta -peptide, S100/calgranulin family proteins, high mobility group B1 (HMGB1, also know as amphoterin) and leukocyte integrins (1, 2).

The human RAGE gene encodes a 404 amino acid residues (aa) type I transmembrane glycoprotein with a 22 aa signal peptide, a 320 aa extracellular domain containing an Ig-like V-type domain and two Ig-like Ce-type domains, a 21 aa transmembrane domain and a 41 aa cytoplasmic domain (3). The V-type domain and the cytoplasmic domain are important for ligand binding and for intracellular signaling, respectively. Two alternative splice variants, lacking the V-type domain or the cytoplasmic tail, are known (1, 4). RAGE is highly expressed in the embryonic central nervous system (5). In adult tissues, RAGE is expressed at low levels in multiple tissues including endothelial and smooth muscle cells, mononuclear phagocytes, pericytes, microglia, neurons, cardiac myocytes and hepatocytes (6). The expression of RAGE is upregulated upon ligand interaction. Depending on the cellular context and interacting ligand, RAGE activation can trigger differential signaling pathways that affect divergent pathways of gene expression (1, 7). RAGE activation modulates varied essential cellular responses (including inflammation, immunity, proliferation, cellular adhesion and migration) that contribute to cellular dysfunction associated with chronic diseases such as diabetes, cancer, amyloidoses and immune or inflammatory disorders (1).

  1. Schmidt, A. et al. (2001) J. Clin. Invest. 108:949.
  2. Chavakis, T. et al. (2003) J. Exp. Med. 198:507.
  3. Neeper, M. et al. (1992) J. Biol. Chem. 267:14998.
  4. Yonekura, H. et al. (2003) Biochem. J. 370:1097.
  5. Hori, O. et al. (1995) J. Biol. Chem. 270:25752.
  6. Brett, J. et al. (1993) Am. J. Pathol. 143:1699.
  7. Valencia, J.V. et al. (2004) Diabetes 53:743.
Long Name
Receptor for Advanced Glycation End Products
Entrez Gene IDs
177 (Human); 11596 (Mouse); 81722 (Rat); 403168 (Canine)
Alternate Names
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

Citations for Recombinant Human RAGE Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

19 Citations: Showing 1 - 10
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  1. Selecting Multitarget Peptides for Alzheimer's Disease
    Authors: A Kasus-Jaco, JL Washburn, RB Laurence, HA Pereira
    Biomolecules, 2022-09-27;12(10):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: ELISA Standard
  2. AIM/CD5L attenuates DAMPs in the injured brain and thereby ameliorates ischemic stroke
    Authors: N Maehara, K Taniguchi, A Okuno, H Ando, A Hirota, Z Li, CT Wang, S Arai, T Miyazaki
    Cell Reports, 2021-09-14;36(11):109693.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Venestatin from parasitic helminths interferes with receptor for advanced glycation end products (RAGE)-mediated immune responses to promote larval migration
    Authors: D Tsubokawa, T Kikuchi, JM Lee, T Kusakabe, Y Yamamoto, H Maruyama
    PloS Pathogens, 2021-06-03;17(6):e1009649.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  4. Hydrophobicity drives receptor-mediated uptake of heat-processed proteins by THP-1 macrophages and dendritic cells, but not cytokine responses
    Authors: Y Deng, C Govers, M Teodorowic, I Liobyte, I De Simone, K Hettinga, HJ Wichers
    PLoS ONE, 2020-08-14;15(8):e0236212.
    Species: Bovine
    Sample Types: Protein
    Applications: Bioassay
  5. HMGB1 promotes hair growth via the modulation of prostaglandin metabolism
    Authors: JH Hwang, H Chu, Y Ahn, J Kim, DY Kim
    Sci Rep, 2019-04-30;9(1):6660.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. HMGB1-containing nucleosome mediates chemotherapy-induced metastasis of human lung cancer
    Authors: K Wang, S Shan, S Wang, X Gu, X Zhou, T Ren
    Biochem. Biophys. Res. Commun., 2018-04-24;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. TREM2 Is a Receptor for ?-Amyloid that Mediates Microglial Function
    Authors: Y Zhao, X Wu, X Li, LL Jiang, X Gui, Y Liu, Y Sun, B Zhu, JC Piña-Cresp, M Zhang, N Zhang, X Chen, G Bu, Z An, TY Huang, H Xu
    Neuron, 2018-03-07;97(5):1023-1031.e7.
    Species: Human
    Sample Types: Recominant Protein
    Applications: Bioassay
  8. A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense
    Authors: D Wolf, N Anto-Miche, H Blankenbac, A Wiedemann, K Buscher, JD Hohmann, B Lim, M Bäuml, A Marki, M Mauler, D Duerschmie, Z Fan, H Winkels, D Sidler, P Diehl, DM Zajonc, I Hilgendorf, P Stachon, T Marchini, F Willecke, M Schell, B Sommer, C von Zur Mu, J Reinöhl, T Gerhardt, EF Plow, V Yakubenko, P Libby, C Bode, K Ley, K Peter, A Zirlik
    Nat Commun, 2018-02-06;9(1):525.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Therapeutic potential of targeting S100A11 in malignant pleural mesothelioma
    Authors: H Sato, M Sakaguchi, H Yamamoto, S Tomida, K Aoe, K Shien, T Yoshioka, K Namba, H Torigoe, J Soh, K Tsukuda, H Tao, K Okabe, S Miyoshi, HI Pass, S Toyooka
    Oncogenesis, 2018-01-24;7(1):11.
    Species: Human
    Sample Types: Whole Cells
  10. High mobility group box-1 contributes to anti-myeloperoxidase antibody-induced glomerular endothelial cell injury through a moesin-dependent route
    Authors: H Deng, C Wang, DY Chang, N Hu, M Chen, MH Zhao
    Arthritis Res. Ther., 2017-06-06;19(1):125.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Characterization of ?X I-Domain Binding to Receptors for Advanced Glycation End Products (RAGE)
    Authors: D Buyannemek, SU Nham
    Mol. Cells, 2017-05-24;40(5):355-362.
    Applications: Bioassay
  12. The Role of Neutrophil Proteins on the Amyloid Beta-RAGE Axis
    PLoS ONE, 2016-09-27;11(9):e0163330.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  13. High-mobility group box 1 accelerates lipopolysaccharide-induced lung fibroblast proliferation in vitro: involvement of the NF-kappaB signaling pathway.
    Authors: Li W, Xu Q, Deng Y, Yang Z, Xing S, Zhao X, Zhu P, Wang X, He Z, Gao Y
    Lab Invest, 2015-04-13;95(6):635-47.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  14. Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12.
    Authors: Augner K, Eichler J, Utz W, Pischetsrieder M
    PLoS ONE, 2014-11-26;9(11):e113418.
    Species: Bacteria - E. Coli
    Sample Types: Protein
    Applications: Surface Plasmon Resonance
  15. Low anticoagulant heparin targets multiple sites of inflammation, suppresses heparin-induced thrombocytopenia, and inhibits interaction of RAGE with its ligands.
    Authors: Rao NV, Argyle B, Xu X, Reynolds PR, Walenga JM, Prechel M, Prestwich GD, MacArthur RB, Walters BB, Hoidal JR, Kennedy TP
    Am. J. Physiol., Cell Physiol., 2010-04-07;299(1):C97-110.
    Species: Human
    Sample Types: Protein, Recombinant Protein, Whole Cells
    Applications: Binding Assay, ELISA (Capture)
  16. Evolutionarily conserved recognition and innate immunity to fungal pathogens by the scavenger receptors SCARF1 and CD36.
    Authors: Means TK, Mylonakis E, Tampakakis E, Colvin RA, Seung E, Puckett L, Tai MF, Stewart CR, Pukkila-Worley R, Hickman SE, Moore KJ, Calderwood SB, Hacohen N, Luster AD, El Khoury J
    J. Exp. Med., 2009-02-23;206(3):637-53.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  17. S100A11, an dual mediator for growth regulation of human keratinocytes.
    Authors: Sakaguchi M, Sonegawa H, Murata H, Kitazoe M, Futami J, Kataoka K, Yamada H, Huh NH
    Mol. Biol. Cell, 2007-10-31;19(1):78-85.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  18. Increase in production of matrix metalloproteinase 13 by human articular chondrocytes due to stimulation with S100A4: Role of the receptor for advanced glycation end products.
    Authors: Yammani RR, Carlson CS, Bresnick AR, Loeser RF
    Arthritis Rheum., 2006-09-01;54(9):2901-11.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  19. Molecular mechanisms of Ca(2+) signaling in neurons induced by the S100A4 protein.
    Authors: Kiryushko D, Novitskaya V, Soroka V, Klingelhofer J, Lukanidin E, Berezin V, Bock E
    Mol. Cell. Biol., 2006-05-01;26(9):3625-38.
    Species: Rat
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance


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Recombinant Human RAGE Fc Chimera Protein, CF
By Balaji Mahender on 12/20/2017
Application: Immunoassay Standard