Acetylation modification of proteins is a special class of post-translational modifications of proteins in which acetyl groups are added to lysine residues of proteins by the action of acetyltransferases, a mechanism for cellular control of gene expression, protein activity, or physiological processes. Acetylation is mainly focused on the effects on cellular chromosome structure and activation of transcriptional regulators in the nucleus and is also involved in cell cycle and metabolism, and actin polymerization control.

What We Offer

Lifeasible provides qualitative and quantitative analysis of the acetylated plant proteome to researchers worldwide by identifying acetylated proteins and corresponding acetylation sites in plant tissue and cell samples. Samples are enzymatically cleaved and specifically enriched for acetylated peptides in complex samples using motif antibodies with high affinity for acetylated lysine (Ac-K), which are then analyzed by high-precision mass spectrometry. The mass spectrometry technique and enrichment processing enable qualitative and quantitative analysis of acetylated proteins on a large scale.

Service Flow

Sample Requirement

➢ Plant leaves >5 g

➢ Plant rhizome, xylem, bast >8 g

* If you are providing tissue samples, please send us the tissue samples on dry ice.

* If you are providing protein samples, protein extraction can be done with normal tissue and cell lysis solution.

Technical Characteristics

➢ We use peptide pre-separation to reduce the effect of high abundance histones on protein acetylation identification, and then enrich the acetylated peptides by efficient antibodies to achieve large-scale acetylation identification and quantification.

➢ To identify and quantify more acetylated peptides, we use 2-3 different enzymes for protein samples during the enzymatic digestion process to ensure that peptides with acetylation sites are ionized with high efficiency into the mass spectrometry for analysis, excluding the loss of acetylation information due to inappropriate peptide length and low ionization efficiency.

Reference

1. Iris F., et al. “Proteins of Diverse Function and Subcellular Location Are Lysine Acetylated in Arabidopsis.” Plant Physiology, 2011, 155(4): 1779-1790.

*If your organization requires the signing of a confidentiality agreement, please contact us by email.

For research or industrial use.

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