Serving Your Proteomics Needs
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)|
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
Protein / Anti-Succinyl-Lysine
If you are interested, please follow these steps to obtain more information and order this service.