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AB125158

Anti-MGO-modified proteins antibody [MGO-1]

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(1 Publication)

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, WB

applications

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
Preservative: 0.02% Sodium azide Constituents: 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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 43:531-541 PubMed36545833

2022

Role of post-ischemic phase-dependent modulation of anti-inflammatory M2-type macrophages against rat brain damage.

Applications

Unspecified application

Species

Unspecified reactive species

Yoshitaka Kurashiki,Hiroshi Kagusa,Kenji Yagi,Tomoya Kinouchi,Manabu Sumiyoshi,Takeshi Miyamoto,Kenji Shimada,Keiko T Kitazato,Yoshihiro Uto,Yasushi Takagi
View all publications

Product promise

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