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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 Kits (71) and Advanced Glycosylation End Product-Specific Receptor Proteins (34) and many more products for this protein.
Showing 10 out of 323 products:
Cow (Bovine) Polyclonal AGER Primary Antibody for EIA, IHC (p) - ABIN264840
Sugars, Karlström, Christersson, Olsson, Wendel, Fried: Expression of HMGB1 during tooth development. in Cell and tissue research 2007
Show all 5 references for ABIN264840
Human Polyclonal AGER Primary Antibody for IHC (p), WB - ABIN389027
Schlueter, Hauke, Flohr, Rogalla, Bullerdiek: Tissue-specific expression patterns of the RAGE receptor and its soluble forms--a result of regulated alternative splicing? in Biochimica et biophysica acta 2003
Show all 4 references for ABIN389027
Human Polyclonal AGER Primary Antibody for IF, IHC (p) - ABIN1108826
Bierhaus, Haslbeck, Humpert, Liliensiek, Dehmer, Morcos, Sayed, Andrassy, Schiekofer, Schneider, Schulz, Heuss, Neundörfer, Dierl, Huber, Tritschler, Schmidt, Schwaninger, Haering, Schleicher, Kasper et al.: Loss of pain perception in diabetes is dependent on a receptor of the immunoglobulin superfamily. ... in The Journal of clinical investigation 2004
Show all 4 references for ABIN1108826
Human Polyclonal AGER Primary Antibody for EIA, IHC (p) - ABIN357685
Shanmugam, Kim, Lanting, Natarajan: Regulation of cyclooxygenase-2 expression in monocytes by ligation of the receptor for advanced glycation end products. in The Journal of biological chemistry 2003
Show all 3 references for ABIN357685
Human Polyclonal AGER Primary Antibody for EIA, IHC (p) - ABIN359696
Miyata, Akashi, Nishida: Molecular cloning and characterization of a novel member of the MAP kinase superfamily. in Genes to cells : devoted to molecular & cellular mechanisms 1999
Show all 2 references for ABIN359696
Human Polyclonal AGER Primary Antibody for WB - ABIN2786877
Luo, Saiardi, Nagata, Ye, Yu, Jung, Luo, Jain, Sawa, Snyder: GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase. in Neuron 2001
Show all 2 references for ABIN2786877
Human Polyclonal AGER Primary Antibody for IHC, WB - ABIN2776917
Lieuw-a-Fa, Schalkwijk, Engelse, van Hinsbergh: Interaction of Nepsilon(carboxymethyl)lysine- and methylglyoxal-modified albumin with endothelial cells and macrophages. Splice variants of RAGE may limit the responsiveness of human endothelial cells to AGEs. in Thrombosis and haemostasis 2006
Human Polyclonal AGER Primary Antibody for IF, WB - ABIN390897
Peng, Lu, Wang, Yan, Chen, Zhang, Zhang, Shen: RAGE gene polymorphisms are associated with circulating levels of endogenous secretory RAGE but not with coronary artery disease in Chinese patients with type 2 diabetes mellitus. in Archives of medical research 2009
Human Polyclonal AGER Primary Antibody for FACS, IHC (p) - ABIN651054
Rojas, Figueroa, Morales: Fueling inflammation at tumor microenvironment: the role of multiligand/RAGE axis. in Carcinogenesis 2010
Elevated serum RAGE level is Associated with Metabolic Syndrome.
RAGE polymorphism is associated with an increased risk of coronary artery disease and ischemic stroke.
These data imply that RAGE promotes the growth of Osteosarcoma (OS)and is a potential diagnostic biomarker and therapeutic target for the disorder
hA17-29 aggregate toxicity seems to be mediated by RAGE and p75-NGFR (show NGFR Antibodies) receptors
Data show that advanced glycation end-products (RAGE) is equally expressed in both macrophage phenotypes and that RAGE activation by high-mobility group (show SSRP1 Antibodies) protein box1 (HMGB1 (show HMGB1 Antibodies)) promotes protumoral activities of M2 macrophages.
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 Antibodies) 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
Our results suggested that the increased RAGE expression in inflammatory circumstances and interaction with AGEs are risk factors in decreasing of aggrecan (show ACAN Antibodies) content in nucleus pulposus.
These findings suggest that the inhibitory effect of these plant extracts on the activation of AGEs/RAGE/SphK1 (show SPHK1 Antibodies) signaling pathway in db/db (show LEPR Antibodies) diabetic mice kidney is a novel mechanism by which they exert renoprotective effects in diabetic nephropathy.
Small Molecule Inhibition of Ligand-Stimulated RAGE-DIAPH1 (show DIAPH1 Antibodies) Signal Transduction.
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 Antibodies) levels both in vivo and in vitro, and reducing RAGE level in the blood-brain barrier model in vitro
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 Antibodies)/LPS (show TLR4 Antibodies)-induced liver injury through down-regulation of the TLR4 (show TLR4 Antibodies) 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 Antibodies) and its main receptor, RAGE, appear to be crucial factors in the pathogenesis of TnI (show TNNI2 Antibodies)-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.
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