Description
Recombinant Human AGER/RAGE Protein (His Tag) | PKSH032048 | Gentaur US, UK & Europe Disrtribition
Synonyms: Advanced Glycosylation End Product-Specific Receptor; Receptor for Advanced Glycosylation End Products; AGER; RAGE
Active Protein: N/A
Activity: Recombinant Human Advanced Glycosylation End Product-Specific Receptor is produced by our Mammalian expression system and the target gene encoding Ala23-Ala344 is expressed with a 6His tag at the C-terminus.
Protein Construction: Recombinant Human Advanced Glycosylation End Product-Specific Receptor is produced by our Mammalian expression system and the target gene encoding Ala23-Ala344 is expressed with a 6His tag at the C-terminus.
Fusion Tag: C-6His
Species: Human
Expressed Host: Human Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 35.2 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Reconstitution: Please refer to the printed manual for detailed information.
Background: Advanced Glycosylation End Product-Specific Receptor (AGER) belongs to the immunoglobulin superfamily of cell surface molecules. It lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Besides AGEs, AGER is also able to bind other ligands which is thought to result in pro-inflammatory gene activation. It is known that AGER serve as a mediator of both acute and chronic vascular inflammation in certain conditions such as atherosclerosis and in particular as a complication of diabetes. Furthermore, it plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes.
Research Area: Cardiovascular, Neuroscience
