Analytical Data
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Gene name
AGER
- Application
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Alternative Names
AGER；RAGE；Advanced glycosylation end product-specific receptor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15109
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Expression Region
23-344aa
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AA Sequence
AQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALA
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Molecular Weight
36.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
AGER, or Advanced Glycation End-Product Receptor, is a crucial member of the immunoglobulin superfamily that plays a significant role in various pathological conditions, including diabetes, inflammation, and neurodegenerative diseases. Research into AGER has expanded in recent years due to its involvement in the cellular responses to advanced glycation end-products (AGEs), which are harmful compounds formed during the metabolism of carbohydrates and proteins. The binding of AGEs to AGER activates several signaling pathways that can lead to chronic inflammation and tissue damage, thereby contributing to the progression of diseases such as diabetic complications, atherosclerosis, and Alzheimer's disease. Studies have shown that modulating the activity of AGER can provide potential therapeutic strategies to counteract the detrimental effects of AGEs. Consequently, the recombinant expression of AGER is being explored to better understand its functional mechanisms, structure-function relationships, and to develop novel treatments. By producing recombinant AGER proteins, researchers aim to unravel the receptor's physiological roles, characterize its ligand-binding properties, and assess how manipulating its pathways can mitigate disease symptoms and improve health outcomes. This research is particularly relevant in the context of developing targeted therapies aimed at reducing AGE accumulation and its associated health problems, highlighting AGER as a promising target for novel pharmacological interventions.
