Mouse AGER Protein 3289

$255.00 – $850.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Gly23-Ala340

SKU: 3289parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_031451.2
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	The receptor for advanced glycation end-products (RAGE) is a cell surface transmembrane multiligand receptor, encoded by the AGER gene. RAGE presents many transcripts, is expressed mainly in the lung, and involves multiple pathways (such as NFκB, Akt, p38, and MAP kinases) that initiate and perpetuate an unfavorable proinflammatory state.
molecular weight	The protein has a predicted MW of 34.85 kDa. Due to glycosylation, the protein migrates to 45-50 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Mouse AGER Protein 3289

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
The receptor for advanced glycation end-products (RAGE) is a cell surface transmembrane multiligand receptor, encoded by the AGER gene. RAGE presents many transcripts, is expressed mainly in the lung, and involves multiple pathways (such as NFκB, Akt, p38, and MAP kinases) that initiate and perpetuate an unfavorable proinflammatory state.
Protein names Advanced glycosylation end product-specific receptor (Receptor for advanced glycosylation end products)
Mass 42803Da
Function Cell surface pattern recognition receptor that senses endogenous stress signals with a broad ligand repertoire including advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, phospholipids and glycosaminoglycans (PubMed:27572515, PubMed:28515150, PubMed:34743181). Advanced glycosylation end products are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes (PubMed:21565706). These ligands accumulate at inflammatory sites during the pathogenesis of various diseases, including diabetes, vascular complications, neurodegenerative disorders, and cancers and RAGE transduces their binding into pro-inflammatory responses. Upon ligand binding, uses TIRAP and MYD88 as adapters to transduce the signal ultimately leading to the induction or inflammatory cytokines IL6, IL8 and TNFalpha through activation of NF-kappa-B (PubMed:21829704). Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators (PubMed:19386136). Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons (PubMed:19906677). 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. Participates in endothelial albumin transcytosis together with HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial hyperpermeability (PubMed:27572515). Mediates the loading of HMGB1 in extracellular vesicles (EVs) that shuttle HMGB1 to hepatocytes by transferrin-mediated endocytosis and subsequently promote hepatocyte pyroptosis by activating the NLRP3 inflammasome (PubMed:34743181). Promotes also extracellular hypomethylated DNA (CpG DNA) uptake by cells via the endosomal route to activate inflammatory responses (PubMed:24081950, PubMed:28515150). {ECO:0000250\|UniProtKB:Q62151, ECO:0000269\|PubMed:19906677, ECO:0000269\|PubMed:20943659, ECO:0000269\|PubMed:21559403, ECO:0000269\|PubMed:21565706, ECO:0000269\|PubMed:21829704, ECO:0000269\|PubMed:24081950, ECO:0000269\|PubMed:27572515, ECO:0000269\|PubMed:28515150, ECO:0000269\|PubMed:34743181}.
Subellular location [Isoform 1]: Cell membrane {ECO:0000269\|PubMed:24081950, ECO:0000269\|PubMed:27572515}; Single-pass type I membrane protein.; [Isoform 2]: Secreted.; [Isoform 10]: Cell membrane {ECO:0000269\|PubMed:24260107}; Single-pass type I membrane protein {ECO:0000269\|PubMed:24260107}.
Tissues Endothelial cells.
Structure Constitutive homodimer; disulfide-linked (PubMed:24081950). Forms homooligomers (PubMed:24081950). Interacts with S100A1 and APP (By similarity). Interacts with S100B, S100A12 and S100A14. Interacts with TIRAP (PubMed:21829704). Interacts with HMGB1 (PubMed:34743181). {ECO:0000250\|UniProtKB:Q62151, ECO:0000269\|PubMed:19386136, ECO:0000269\|PubMed:20943659, ECO:0000269\|PubMed:20947022, ECO:0000269\|PubMed:21559403, ECO:0000269\|PubMed:21565706, ECO:0000269\|PubMed:21829704, ECO:0000269\|PubMed:23284645, ECO:0000269\|PubMed:24081950, ECO:0000269\|PubMed:34743181}.
Post-translational modification Phosphorylated on its cytoplasmic domain by PKCzeta/PRKCZ upon ligand binding. {ECO:0000269\|PubMed:21829704}.; Targeted by the ubiquitin E3 ligase subunit FBXO10 to mediate its ubiquitination and degradation. {ECO:0000269\|PubMed:28515150}.
Target Relevance information above includes information from UniProt accession: Q15109
The UniProt Consortium

Data

The purity of Mouse AGER is greater than 95% as determined by SEC-HPLC.

Mouse AGER on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.