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The advanced glycosylation end product (AGE) receptor encoded by AGER is a member of the immunoglobulin superfamily of cell surface receptors. Additionally we are shipping Advanced Glycosylation End Product-Specific Receptor Antibodies (319) and Advanced Glycosylation End Product-Specific Receptor Kits (71) and many more products for this protein.
Showing 10 out of 39 products:
Human AGER Protein expressed in Human Cells - ABIN2004449
Sugaya, Fukagawa, Matsumoto, Mita, Takahashi, Ando, Inoko, Ikemura et al.: Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart ... in Genomics 1995
Show all 4 references for ABIN2004449
Mouse (Murine) AGER Protein expressed in Human Cells - ABIN2007883
Neeper, Schmidt, Brett, Yan, Wang, Pan, Elliston, Stern, Shaw: Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. in The Journal of biological chemistry 1992
Show all 4 references for ABIN2007883
Human AGER Protein expressed in HEK-293 Cells - ABIN2180572
Xue, Rai, Singer, Chabierski, Xie, Reverdatto, Burz, Schmidt, Hoffmann, Shekhtman: Advanced glycation end product recognition by the receptor for AGEs. in Structure (London, England : 1993) 2011
Show all 3 references for ABIN2180572
increased soluble RAGE levels and Gly82Ser polymorphism either combinatorially or seperately increased the propensity towards obesity.
RAGE has been identified as a novel binding protein for BLT1; RAGE modulates downstream signaling from BLT1 and affects cell migration through BLT1 both in vitro and in vivo.
The present study revealed that the RAGE G82S polymorphism was associated with chronic periodontitis in the non-diabetes mellitus group but not in the diabetes mellitus group.
Interaction of extracellular S100A4 (show S100A4 Proteins) with RAGE prompts prometastatic activation of melanoma cells.
Down-regulation of soluble RAGE and its association with acute phase response suggest a role for RAGE activation in the pathogenesis of chronic spontaneous urticaria
RAGE -374T/A correlates with microalbuminuria onset in the French DT1 cohort.
Data suggest that proteolysis of receptor for advanced glycation end products (RAGE) is critical to mediate signaling and cell function and may emerge as a therapeutic target for RAGE-dependent disease states.
Study demonstrated that 1,25(OH)2D3, the active form of vitamin D, plays an important role in increasing Abeta1-40 vectorial transport from the brain to blood and systemic clearance from peripheral circulation through increasing LRP1 (show LRP1 Proteins) levels both in vivo and in vitro, and reducing RAGE level in the blood-brain barrier model in vitro
Genetically lowered concentrations of circulating AGER might cause an increased risk of cancer. (Meta-analysis)
preliminary evidence in a Chinese population that the RAGE polymorphism is involved in genetic susceptibility to ulcerative colitis
Our results suggested that the increased RAGE expression in inflammatory circumstances and interaction with AGEs are risk factors in decreasing of aggrecan (show ACAN Proteins) content in nucleus pulposus.
Small Molecule Inhibition of Ligand-Stimulated RAGE-DIAPH1 (show DIAPH1 Proteins) Signal Transduction.
This present study confirmed an important role of RAGE in vivo and vitro models of pulmonary fibrosis and suggested the therapeutic possibility for pulmonary fibrosis via RAGE regulation
beta-Caryophyllene protects against GalN (show GAL Proteins)/LPS (show TLR4 Proteins)-induced liver injury through down-regulation of the TLR4 (show TLR4 Proteins) and RAGE signaling.
AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
HMGB1 (show HMGB1 Proteins) and its main receptor, RAGE, appear to be crucial factors in the pathogenesis of TnI (show TNNI2 Proteins)-induced experimental autoimmune myocarditis.
Only one fragment RAGE (60-76) was shown to have a therapeutic activity improving the memory state of bulbectomized mice and leads to decreasing in the level of brain beta-amyloid.
These data implicate RAGE as a modulator of both vasoreactivity and of proliferative processes in the response of the pulmonary circulation to chronic-hypoxia.
activation of the RAGE by advanced glycation end products or other ligands suppresses NIPP1 (show PPP1R8 Proteins) expression in diabetic nephropathy, contributes to podocyte hypertrophy, and glomerular inflammation
The advanced glycosylation end product (AGE) receptor encoded by this gene is a member of the immunoglobulin superfamily of cell surface receptors. It is a multiligand receptor, and besides AGE, interacts with other molecules implicated in homeostasis, development, and inflammation, and certain diseases, such as diabetes and Alzheimer's disease. Many alternatively spliced transcript variants encoding different isoforms, as well as non-protein-coding variants, have been described for this gene (PMID:18089847).
advanced glycosylation end product-specific receptor
, RAGE isoform NtRAGE-delta
, RAGE isoform sRAGE-delta
, advanced glycation end product receptor
, advanced glycosylation end product-specific receptor variant 1
, advanced glycosylation end product-specific receptor variant 3
, advanced glycosylation end product-specific receptor variant 4
, advanced glycosylation end product-specific receptor variant 5
, advanced glycosylation end product-specific receptor variant 6
, advanced glycosylation end product-specific receptor variant 7
, advanced glycosylation end product-specific receptor variant 8
, receptor for advanced glycosylation end products
, advanced glycation end-products receptor
, advanced glycosylation end product-specific receptor variant 2