Description
Key facts
Purity:>98% SDS-PAGE,
Expression system:Native,
Tags:Tag free,
Applications:SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Animal free:No,
Carrier free:Yes,
Storage buffer:Constituents: PBS
Product details:
The AGE modified BSA was produced by reacting BSA with glycolaldehyde under sterile conditions followed by extensive dialysis and purification steps.
ab51995 may precipitate during extended storage. Sonicate to solubilize the precipitates.
Fluorescence of AGEs was confirmed by fluorescence spectrophotometry with Ex/Em = 370/440 nm.
Glycated BSA shows a 7000% increase in fluorescence in compared to control BSA.
Ensure the validity of your result using our AGE-BSA protein ab51995 as a positive control in SDS-PAGE.
Check out our protein gel staining guide for SDS-PAGE
This product is manufactured by BioVision, an Abcam company and was previously called 2221 AGE-BSA. 2221-10 is the same size as the 10 mg size of ab51995.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Advanced Glycation End-products (AGEs) are highly reactive compounds formed when reducing sugars non-enzymatically bind to proteins lipids or nucleic acids. They are often referred to as AGE products or AGE-BSA when in the form of bovine serum albumin (BSA). The molecular weight of AGE compounds can vary significantly due to the diversity of glycation products. AGEs express in various tissues but accumulate more in aging tissues and in certain pathological states. Detection of AGE products often utilizes AGE ELISA assays or fluorescence-based methods to measure AGE-BSA.
Biological function summary
AGE compounds affect cellular and tissue functions by altering structural proteins and increasing oxidative stress. While not a component of a specific complex AGEs catalyze cross-linking of proteins like collagen impacting tissue elasticity. The binding of AGEs to receptors such as RAGE (Receptor for Advanced Glycation End-products) triggers inflammatory pathways and oxidative stress. This interaction fuels the damaging effects of AGEs in biological systems which are assayed through AGE assays.
Pathways
AGE compounds influence several critical biological pathways particularly the NF-kB and MAPK pathways. These pathways mediate inflammation and cellular stress responses. The interaction with RAGE also affects signaling with related proteins like S100/calgranulins which further activate pro-inflammatory responses. The alteration of these pathways by AGE compounds highlights their significance in cellular dysfunction and age-related conditions.
AGE compounds play significant roles in the progression of diabetes and cardiovascular disease. In diabetes AGEs contribute to complications by modifying vascular structure and function where they link with proteins such as HbA1c in glycation. In cardiovascular disease AGE accumulation in vascular tissues enhances vascular stiffness and atherosclerotic lesion formation. The AGE-RAGE interaction perpetuates chronic inflammation further exacerbating these conditions.
