Lysine propionylation is a newly discovered type of acylation that can occur in a variety of proteins, including
histones and non-histones. Lysine propionylation has been found to play an important regulatory role in both
eukaryotes and prokaryotes. As a newly discovered reversible post-translational modification (PTM) of protein, its
function remains to be investigated in depth and has great potential for research. At present, lysine propionylation
has been reported to take part in a range of biological processes and cellular metabolic pathways in prokaryotes and
eukaryotes, such as bacteria metabolic and metabolic enzyme activity regulatory, bacteria and mammal cellular stress
response, epigenetic regulation, and so on. Creative Proteomics offers the lysine propionylation
analysis service to identify propionylated proteins and their modification sites in a reliable and effective manner.
Protein propionylation
Lysine propionylation is a short-chain acylation of lysine residues in cellular proteins by adding a propionyl group
(CH3-CH2-CO-) to the ɛ-amino group of the lysine residue. Compared to acetylation, lysine propionylation is bulkier
and more hydrophobic due to one or two additional methylene groups, but their chemical properties are similar.
Current research on lysine propionylation is focused on the identification of propionylated proteins in prokaryotes
(e.g., Thermus thermophilus, Mycobacterium tuberculosis, Cyanobacteria, and yeast) and eukaryotes, and on the
enzymes that regulate this modification. The studied enzymes responsible for the addition and removal of lysine
propionylation, such as CREB-binding protein, AcuA, CobB, p300, Sirt1/2/3, etc. These studies suggest that lysine
propionylation occurs in a wide range of proteins and has implications for a variety of biological functions. In
particular, lysine propionylation may be one of the mechanisms that regulate cellular metabolism and response to
stressful conditions in bacteria and mammals.
Proteomics analysis of propionylation
Creative Proteomics combines high-affinity anti-alanyl lysine pan-antibodies with high-precision
mass spectrometry (MS) analysis to provide comprehensive and accurate identification of lysine propionylated
proteins and lysine propionylation sites in a variety of bacterial and mammalian cells. Our strong bioinformatics
team provides standard and advanced bioinformatics services to meet a wide range of bioinformatics needs. With our
well-established platform, we also provide functional validation services for propionylated proteins. Specifically,
our service can help our customers to achieve the following lists:
- Identification of lysine propionylated proteins.
- Functional annotation of propionylated proteins.
- Identification and analysis of lysine propionylated sites.
- Functional validation of lysine propionylated proteins.
Sample requirements
- Acceptable samples: Protein extracts, cell samples, tissue samples, and microorganism samples.
- Sample shipping: Sufficient amount of dry ice for shipping, or consult our technical staff before sending
samples.
- Before the formal experiment, we will always test the samples you provide.
Workflow of protein propionylation analysis
Applications of our protein propionylation analysis
- Fungal/bacterial growth cycle.
- Fungal/bacterial Metabolic regulation.
- Bacteria and mammal cellular stress response.
- Mitochondrial research.
- Biosynthesis.
- Chromatin activation.
- Oxygenic photosynthesis.
You only need to place an order and send samples, we provide one-stop services. Please contact us if you are interested. We are looking forward to cooperating with you.
Reference
- Okanishi, Hiroki, et al. "Lysine propionylation is a prevalent post-translational modification in
Thermus thermophilus." Molecular & Cellular Proteomics 13.9 (2014): 2382-2398.
Our products and services are for research use only.
