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Detection of Lysine Succinylation (Ksucc) by 2D Western Blot




Lysine Succinylation (Ksucc) is a common post-translational modifications and occurs in a wide range of proteins. The addition of succinyl group changes lysine's charge from +1 to −1 and introduces a relatively large structural moiety (100 Da), bigger than acetylation (42 Da) or methylation (14 Da). Numerous proteins involved in the regulation of cellular and biological processes have been shown to be heavily succinylated. Emerging clinical data provides evidence that dysregulation of Ksucc is correlated with the development of cardiovascular diseases and cancer. Applied Biomics’ 2D Fluorescent Western Blot platform offers high sensitivity detection and accurate quantitation of Succinylation in any protein samples.

Here are some representative applications:

1. Phosphorylation 6. Nitrotyrosine
2. Ubiquitination 7. Biotinylation
3. Acetylated-Lysine 8. Succinyl-Lysine
4. Sulfo-Tyrosine 9. Citrullination
5. Methyl-Arginine 10. 4-hydroxynonenal (4-HNE)

8. Succinyl-Lysine

Example: Mouse liver

Lysine succinylation (Ksucc) has a significant impact on protein folding and functions. Proteins from drug treated Mouse liver were extracted, followed by 2D DIGE Western blot using Applied Biomics’ protocols.


Mouse liver protein

PTM 2D Western Blot Lysine Succinylation


PTM 2D Western Blot Lysine Succinylation

Protein / Anti-Succinyl-Lysine

PTM 2D Western Blot Lysine Succinylation

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