Mouse AGER(Advanced Glycosylation End Product Specific Receptor) ELISA Kit
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Product specifications
| Category | ELISA Kits |
| Reactivity | mouse |
| Detection Method | Colorimetric |
| Assay Data | Quantitative |
| Assay Type | Sandwich ELISA, Double Antibody |
| Test Range | 125-8000pg/ml |
| Size 1 | 96T |
| Sample Type | Serum,Plasma,Tissue homogenates,Other biological fluids |
| Availability | Shipped within 10-14 working days. |
| Storage | 2-8 °C for 6 months |
| UniProt ID | Q62151 |
| Alias | RAGE,SCARJ1,sRAGE |
| Background | Elisa Kits AGER |
| Status | RUO |
AGER, also known as RAGE (Receptor for Advanced Glycation End Products), is a transmembrane receptor belonging to the immunoglobulin superfamily that binds to AGEs and other ligands such as S100 proteins, HMGB1, and amyloid-β. AGER is widely expressed, particularly in the endothelium, lungs, brain, and immune cells, and plays a critical role in inflammatory and oxidative stress signaling. Binding of AGEs to AGER activates downstream pathways, including NF-κB, MAPK, and JAK/STAT, leading to the production of pro-inflammatory cytokines and reactive oxygen species. Overexpression or chronic activation of AGER is associated with diseases such as diabetes complications, atherosclerosis, Alzheimer’s disease, and cancer, where it exacerbates inflammation and tissue damage. AGER is a promising therapeutic target for reducing AGE-mediated pathologies and modulating immune and metabolic dysfunction.
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Mouse AGER(Advanced Glycosylation End Product Specific Receptor) ELISA Kit
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anti- AGER antibody
Mediates interactions of advanced glycosylation end products(AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling(By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide(ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase(MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.
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anti- AGER antibody
Mediates interactions of advanced glycosylation end products(AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling(By similarity). Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide(ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase(MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.
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