Recombinant Human Advanced glycosylation end product-specific receptor (AGER), partial
| Product Name | Recombinant Human Advanced glycosylation end product-specific receptor (AGER), partial |
|---|---|
| Description | 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 . Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell mbrane from the Extracellular domain 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 syst delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.4 Publications |
| Synonyms | Receptor for advanced glycosylation end products |
| Host | E.coli |
| Molecular Weight | 38 |
| Amino Acid Sequence | AQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLA |
| Protein Length | Extracellular Domain, 23-342aa |
| Tag | N-terminal 6xHis-tagged |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in Tris-based buffer, 50% glycerol |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| References | Alternative splicing of the RAGE Cytoplasmic domain regulates cell signaling and function.Jules J., Maiguel D., Hudson B.I.PLoS ONE 8:E78267-E78267(2013) |
| Background | 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 . Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell mbrane from the Extracellular domain 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 syst delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides.4 Publications |
| Supplier | Cusabio |
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