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Succinylation Analysis Service

Recently identified as a post-translational modification, succinylation primarily targets lysine residues of proteins and is prevalent in both eukaryotic and prokaryotic cells. Its involvement extends to various metabolic signaling pathways, including the tricarboxylic acid cycle, amino acid metabolism, and fatty acid metabolism. Creative Proteomics is at the forefront, offering top-notch succinylation analysis services, which encompass identification, quantification, and characterization, providing valuable insights that contribute to the advancement of your protein research.

What is Succinylation

Succinylation is a PTM process that alters the structure of a protein by transferring a succinyl group (-CO-CH2-CH2-CO2-CO2-CO2H) to a lysine residue of the target protein. Succinylation can be enzymatic or non-enzymatic, but both ways require succinyl-CoA to provide the succinyl group to be added to the ϵ-amino group of the protein lysine residue. Succinyl-CoA can be produced from either mitochondria or peroxisomes, with mitochondria-produced succinyl-CoA being trapped in the matrix, while peroxisomes-produced succinyl-CoA enters the cytoplasm. This makes it possible for succinylation to occur on both histone and non-histone proteins.

Fig.1 Schematic of succinylation

Fig.1 Schematic of succinylation (Dai, X. et al., 2022)

In comparison to other common covalent modifying groups targeting lysine, such as acetyl and dimethyl, the succinyl group is notably larger and can exert a more pronounced impact on the structure and function of the target protein. Recent research indicates that succinylation is intricately involved in numerous cellular processes, with a plethora of lysine-succinylated proteins identified in the cytoplasm, mitochondria, and nucleus. These proteins include metabolic enzymes participating in the metabolism of fatty acids, amino acids, and carbohydrates, among others. It's noteworthy that while succinylation typically occurs on lysine (K), it can also manifest on arginine (R) or histidine (H) under the influence of varying pH values. Presently, succinylation has emerged as a prevalent post-translational modification in both prokaryotes and eukaryotes, playing a pivotal role in the exploration of proteins and biological processes, among other areas of study.

Applications of Succinylation Analysis

Metabolic Regulation

Succinylation has been implicated in the regulation of metabolic pathways. Key enzymes involved in processes such as the tricarboxylic acid (TCA) cycle have been identified as targets of succinylation, influencing their activity.

Mitochondrial Function

Many succinylated proteins are localized in mitochondria, suggesting a role in the regulation of mitochondrial functions. Succinylation has been associated with the modulation of electron transport chain components and other mitochondrial processes.

Cell Signaling

Succinylation can impact signaling pathways by affecting the activity or stability of signaling proteins. It contributes to the complexity of cellular signaling networks.

Our Service

Creative Proteomics has advanced protein detection technologies and can provide customized services to researchers and scientists to help them reveal the complexity of PTM using powerful mass spectrometry technologies. Our services are thoughtful and detailed and the process of succinylation analysis service is as follows:

Fig.2 Succinylation analysis workflow

Fig.2 Succinylation analysis workflow

Creative Proteomics brings a wealth of experience to the field of protein research. Our comprehensive services and products cover the entire spectrum of utilizing suitable and efficient gateways. Utilizing our proprietary platform, we have successfully implemented many proteomics research projects. If you are interested, please contact us for more information and a quote.

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