Abcam, ab125158, Anti-MGO-modified proteins antibody [MGO-1]

Size: 50µg
Mouse Monoclonal MGO-modified proteins antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Chemical / Small Molecule corresponding to MGO-modified proteins.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:MGO-1,
Isotype:IgG1,
Carrier free:No,
Reacts with:Human,
Applications:IHC-P, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein G, Storage buffer-Preservative: 0.02% Sodium azideConstituents: PBS, 0.1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°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.
MGO-modified proteins also known as methylglyoxal-modified proteins result from the non-enzymatic addition of methylglyoxal a 72 Da aldehyde to proteins. This modification alters the structure and function of proteins by forming advanced glycation end-products (AGEs) and it impacts cellular functions. MGO-modified proteins can be found in various tissues and cells throughout the body reflecting the endogenous and ubiquitous presence of methylglyoxal. Researchers have not significantly associated it with a specific locality in the body but it affects proteins that circulate in the bloodstream including albumin and hemoglobin.
Biological function summary
Proteins that undergo MGO modification can disrupt cellular processes and reduce protein stability. These altered proteins fail to perform their typical functions leading to impairment in protein regulation and cellular signaling. MGO itself does not form part of a complex but its frequent involvement with AGEs allows it to extensively influence cellular mechanisms. The accumulation of MGO-modified proteins can result in oxidative stress and apoptosis in cells further affecting cellular health and functionality.
Pathways
MGO-modified proteins are significantly involved in oxidative stress and the glyoxalase system which detoxifies methylglyoxal using the enzymes glyoxalase I and II. This pathway helps maintain cellular homeostasis by preventing excessive accumulation of MGO and its associated AGEs. MGO-related modifications also play a role in several metabolic pathways impacting proteins like glutathione which is critical for detoxifying reactive species and maintaining redox balance. Their interaction can potentially disrupt normal cellular function if not properly managed.
Proteins modified by MGO link to diabetes and neurodegenerative diseases such as Alzheimer's disease. Elevated levels of MGO and related AGEs have been observed in diabetic patients correlating with microvascular complications. In Alzheimer's disease MGO-modified proteins contribute to amyloid plaque formation which involves amyloid-beta proteins. This modification exacerbates neuronal damage and cognitive decline. MGO's interaction with proteins in these conditions underlines its potential as a therapeutic target to mitigate disease progression and manage symptoms.