Recombinant Human RAGE Fc Chimera Protein, CF

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Human RAGE Fc Chimera Protein, CF Summary

• Details of Functionality: 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.
• Source: Mouse myeloma cell line, NS0-derived human RAGE protein
  

  Human RAGE (Gln24 - Ala344) Accession # Q15109	IEGRMD	Human IgG1 (Pro100 - Lys330)
  N-terminus		C-terminus

• Accession #: Q15109
• 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: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 61 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

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 Human 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 (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.

Publications for AGER (1145-RG)(19)

Publications using 1145-RG

• A Kasus-Jaco, JL Washburn, RB Laurence, HA Pereira Selecting Multitarget Peptides for Alzheimer&#039;s Disease Biomolecules, 2022-09-27;12(10):. 2022-09-27 [PMID: 36291595] (ELISA Standard, Human)
• N Maehara, K Taniguchi, A Okuno, H Ando, A Hirota, Z Li, CT Wang, S Arai, T Miyazaki AIM/CD5L attenuates DAMPs in the injured brain and thereby ameliorates ischemic stroke Cell Reports, 2021-09-14;36(11):109693. 2021-09-14 [PMID: 34525359] (Bioassay, Human)
• D Tsubokawa, T Kikuchi, JM Lee, T Kusakabe, Y Yamamoto, H Maruyama Venestatin from parasitic helminths interferes with receptor for advanced glycation end products (RAGE)-mediated immune responses to promote larval migration PloS Pathogens, 2021-06-03;17(6):e1009649. 2021-06-03 [PMID: 34081755] (Bioassay, Human)
• Y Deng, C Govers, M Teodorowic, I Liobyte, I De Simone, K Hettinga, HJ Wichers Hydrophobicity drives receptor-mediated uptake of heat-processed proteins by THP-1 macrophages and dendritic cells, but not cytokine responses PLoS ONE, 2020-08-14;15(8):e0236212. 2020-08-14 [PMID: 32797100] (Bioassay, Bovine)
• JH Hwang, H Chu, Y Ahn, J Kim, DY Kim HMGB1 promotes hair growth via the modulation of prostaglandin metabolism Sci Rep, 2019-04-30;9(1):6660. 2019-04-30 [PMID: 31040377] (Bioassay, Human)
• K Wang, S Shan, S Wang, X Gu, X Zhou, T Ren HMGB1-containing nucleosome mediates chemotherapy-induced metastasis of human lung cancer Biochem. Biophys. Res. Commun., 2018-04-24;0(0):. 2018-04-24 [PMID: 29679570] (Bioassay, Human)
• 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 TREM2 Is a Receptor for ?-Amyloid that Mediates Microglial Function Neuron, 2018-03-07;97(5):1023-1031.e7. 2018-03-07 [PMID: 29518356] (Bioassay, Human)
• 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 A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense Nat Commun, 2018-02-06;9(1):525. 2018-02-06 [PMID: 29410422] (Bioassay, Human)
• 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 Therapeutic potential of targeting S100A11 in malignant pleural mesothelioma Oncogenesis, 2018-01-24;7(1):11. 2018-01-24 [PMID: 29362358] (Human)
• H Deng, C Wang, DY Chang, N Hu, M Chen, MH Zhao High mobility group box-1 contributes to anti-myeloperoxidase antibody-induced glomerular endothelial cell injury through a moesin-dependent route Arthritis Res. Ther., 2017-06-06;19(1):125. 2017-06-06 [PMID: 28587670] (Bioassay, Human)
• D Buyannemek, SU Nham Characterization of ?X I-Domain Binding to Receptors for Advanced Glycation End Products (RAGE) Mol. Cells, 2017-05-24;40(5):355-362. 2017-05-24 [PMID: 28535664] (Bioassay)
• The Role of Neutrophil Proteins on the Amyloid Beta-RAGE Axis PLoS ONE, 2016-09-27;11(9):e0163330. 2016-09-27 [PMID: 27676391] (Bioassay, Human)
• Li W, Xu Q, Deng Y, Yang Z, Xing S, Zhao X, Zhu P, Wang X, He Z, Gao Y High-mobility group box 1 accelerates lipopolysaccharide-induced lung fibroblast proliferation in vitro: involvement of the NF-kappaB signaling pathway. Lab Invest, 2015-04-13;95(6):635-47. 2015-04-13 [PMID: 25867768] (Bioassay, Mouse)
• Augner K, Eichler J, Utz W, Pischetsrieder M Influence of nonenzymatic posttranslational modifications on constitution, oligomerization and receptor binding of S100A12. PLoS ONE, 2014-11-26;9(11):e113418. 2014-11-26 [PMID: 25426955] (Surface Plasmon Resonance, Bacteria - E. Coli)
• Rao NV, Argyle B, Xu X, Reynolds PR, Walenga JM, Prechel M, Prestwich GD, MacArthur RB, Walters BB, Hoidal JR, Kennedy TP Low anticoagulant heparin targets multiple sites of inflammation, suppresses heparin-induced thrombocytopenia, and inhibits interaction of RAGE with its ligands. Am. J. Physiol., Cell Physiol., 2010-04-07;299(1):C97-110. 2010-04-07 [PMID: 20375277] (Binding Assay, ELISA (Capture), Human)
• 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 Evolutionarily conserved recognition and innate immunity to fungal pathogens by the scavenger receptors SCARF1 and CD36. J. Exp. Med., 2009-02-23;206(3):637-53. 2009-02-23 [PMID: 19237602] (Bioassay, Human)
• Sakaguchi M, Sonegawa H, Murata H, Kitazoe M, Futami J, Kataoka K, Yamada H, Huh NH S100A11, an dual mediator for growth regulation of human keratinocytes. Mol. Biol. Cell, 2007-10-31;19(1):78-85. 2007-10-31 [PMID: 17978094] (Bioassay, Human)
• Yammani RR, Carlson CS, Bresnick AR, Loeser RF 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. Arthritis Rheum., 2006-09-01;54(9):2901-11. 2006-09-01 [PMID: 16948116] (Bioassay, Human)
• Kiryushko D, Novitskaya V, Soroka V, Klingelhofer J, Lukanidin E, Berezin V, Bock E Molecular mechanisms of Ca(2+) signaling in neurons induced by the S100A4 protein. Mol. Cell. Biol., 2006-05-01;26(9):3625-38. 2006-05-01 [PMID: 16612001] (Surface Plasmon Resonance, Rat)

Bioinformatics

• Gene Symbol: AGER
• Uniprot:
  • Q15109()