HEK 293.
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
Greater than 95% as determined by SDS-PAGE.
sRAGE Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 317 amino acids (Gly23–Asp333) and having a molecular mass of 34.0kDa.
sRAGE Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
HEK 293.
GQNITARIGE PLVLSCKGAP KKPPQQLEWK LNTGRTEAWK VLSPQGGPWD SVARILPNGS LLLPATGIVD EGTFRCRATN RRGKEVKSNY RVRVYQIPGK PEIVDPASEL TASVPNKVGT CVSEGSYPAG TLSWHLDGKL LIPDGKETLV KEETRRHPET GLFTLRSELT VIPTQGGTHP TFSCSFSLGL PRRRPLNTAP IQLRVREPGP PEGIQLLVEP EGGIVAPGGT VTLTCAISAQ PPPQVHWIKD GAPLPLAPSP VLLLPEVGHE DEGTYSCVAT HPSHGPQESP PVSIRVTETG DEGPAEGEGL DHHHHHH.
The Advanced Glycosylation End Product-Specific Receptor (AGER), also known as the Receptor for Advanced Glycation End Products (RAGE), is a transmembrane receptor belonging to the immunoglobulin superfamily. It was first characterized in 1992 by Neeper et al. and is known for its ability to bind advanced glycation end products (AGEs), which are glycoproteins modified non-enzymatically through the Maillard reaction .
RAGE is a 35 kilodalton receptor that plays a crucial role in recognizing endogenous stress signals. It has a broad ligand repertoire, including AGEs, S100 proteins, high-mobility group box 1 protein (HMGB1), amyloid beta/APP oligomers, nucleic acids, phospholipids, and glycosaminoglycans . These ligands accumulate at inflammatory sites during the pathogenesis of various diseases, including diabetes, vascular complications, neurodegenerative disorders, and cancers .
The AGER gene is located within the major histocompatibility complex (MHC class III region) on chromosome 6 in humans and chromosome 17 in mice . The gene comprises 11 exons interlaced by 10 introns, with a total length of about 1400 base pairs, including the promoter region . There are multiple isoforms of the RAGE protein, including soluble RAGE (sRAGE), which lacks the transmembrane and signaling domains and is hypothesized to counteract the detrimental action of the full-length receptor .
RAGE is implicated in various diseases due to its pro-inflammatory gene activation upon ligand binding. In diabetes, the enhanced level of RAGE ligands is thought to contribute to diabetic complications . Similarly, RAGE is involved in the pathogenesis of Alzheimer’s disease and certain cancers . The receptor’s ability to detect a class of ligands through a common structural motif makes it a pattern recognition receptor in innate immunity .
Mouse recombinant RAGE is used in research to study the receptor’s function and its role in disease models. By using recombinant technology, scientists can produce RAGE proteins in vitro, allowing for detailed biochemical and structural analyses. This helps in understanding the receptor’s interactions with its ligands and the subsequent signaling pathways involved in disease progression.