Human AGER / RAGE Protein
RAGE
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| Catalog Number | P11629-HCCH |
|---|---|
| Organism Species | Human |
| Host | Human Cells |
| Synonyms | RAGE |
| Molecular Weight | The recombinant human AGER consists of 329 amino acids and predicts a molecular mass of 35 KDa. It migrates as an approximately 46-52 KDa band in SDS-PAGE under reducing conditions. |
| predicted N | Ala 23 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the mature form of human AGER (NP_001127.1) (Met1-Ala 344) was expressed with six amino acids (LEVLFQ) at the C-terminus. |
| Bio-activity | 1. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant human Fc-S100B (P10181-H01H) in a functional ELISA. 2. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant mouse S100B-Fc (P50986-M01H) in a functional ELISA. 3. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant human S100A1-Fc (P10179-H01HE) in a functional ELISA. 4. Measured by its ability to compete with Biotinylated recombinant human AGER for binding to immobilized recombinant human APP-Fc (P10703-H02H) in a functional ELISA. |
| Research Area | Cardiovascular |Atherosclerosis |Vascular Inflammation |Inflammatory mediators |
| Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | Receptor for Advanced Glycosylation End Products (RAGE, or AGER) is a member of the immunoglobulin super-family transmembrane proteins, as a signal transduction receptor which binds advanced glycation endproducts, certain members of the S100/calgranulin family of proteins, high mobility group box 1 (HMGB1), advanced oxidation protein products, and amyloid (beta-sheet fibrils). Initial studies investigating the role of RAGE in renal dysfunction focused on diabetes, neurodegenerative disorders, and inflammatory responses. However, RAGE also has roles in the pathogenesis of renal disorders that are not associated with diabetes, such as obesity-related glomerulopathy, doxorubicin-induced nephropathy, hypertensive nephropathy, lupus nephritis, renal amyloidosis, and ischemic renal injuries. RAGE represents an important factor in innate immunity against pathogens, but it also interacts with endogenous ligands, resulting in chronic inflammation. RAGE signaling has been implicated in multiple human illnesses, including atherosclerosis, arthritis, Alzheimer's disease, atherosclerosis and aging associated diseases. |
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