S-Glutathionylation-Specific Antibody Introduction

S-glutathionylation is the process of forming a mixed disulfide between glutathione and cysteine residues in target proteins. It regulates protein function and is a protein post-translational modification (PTM). S-glutathionylation has been found to be closely associated with various pathological mechanisms in mammalian cells, but the precise regulatory mechanisms remain unclear. Additionally, research on S-glutathionylation in plants is still in its early stage. Utilizing our hybridoma platform and phage display platform, Creative Biolabs offers a comprehensive service for the development of S-glutathionylation-specific antibodies.

S-Glutathionylation Modification

In biological tissues, glutathione can exist in the reduced form. When oxidized,, reduced glutathione converts to oxidized glutathione.Oxidative stress can also lead to reversible S-glutathionylation modification of proteins. The mechanism of S-glutathionylation is based on redox reactions involving proteins containing sulfhydryl groups or GSH. Generally, the reaction mechanism of S-glutathionylation is as follows: 1. Thiol-disulfide exchange occurs between sulfhydryl-containing proteins and oxidized glutathione (GSSG). 2. Intracellular ROS and/or RNS induced the production of protein hypersulfonic acid (P-SOH) or glutathione hypersulfonic acid (GSOH) intermediates, leading to modification. 3. S-glutathionylation modification mediated by hyposulfenamide intermediates. 4. ROS and/or RNS induce the production of sulfur radicals, which are then modified through radical recombination or reaction with thiolates. 5. Similar to hyposulfenate, ROS and/or RNS induce the production of nitrosoglutathione (GSNO) or nitrosoprotein (P-SNO) intermediates, leading to modification. 6. Glutathione-catalyzed modification by S-glutathionylation.

S-glutathionylation can regulate a variety of intracellular physiological or biochemical processes such as oxidative stress, cellular metabolism, transcription and translation, protein folding, free radical scavenging, cell motility, and apoptosis by modulating protein function or activity. Currently, there are six main methods for detecting S-glutathionylation: ³⁵S-Cys radiolabeling, biotin labeling, proteomics, protein S-glutathionylation assay using eosin-labeled oxidized glutathione and SDS-PAGE, antibody method for S-glutathionylation, and clickable reaction and proteomics-based methods for S-glutathionylation.

S-Glutathionylation-Specific Antibody

The development of PTM specific antibodies has been a major challenge in PTM research. S-glutathionylation-specific antibodies often exhibit reduced sensitivity, greatly limiting the sensitivity of S-glutathionylation assays. To overcome this limitation, proteins can be purified or enriched for target proteins during the assay, and higher-quality S-glutathionylation-specific antibodies can be developed using hybridoma technology or phage display technology to meet study's requirements.

Creative Biolabs possesses extensive knowledge and experience in PTM-specific antibody discovery. We are eager to discuss our expertise in S-glutathionylation-specific antibody development with you.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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