Acetylation Analysis Service


Introduction

Acetylation is an important modification of  proteins in cell biology. N-acetylation, or the transfer of an acetyl group to  nitrogen, occurs in almost all eukaryotic proteins through both irreversible  and reversible mechanisms. N-terminal acetylation requires the cleavage of the  N-terminal methionine by methionine aminopeptidase (MAP) before replacing the  amino acid with an acetyl group from acetyl-CoA by N-acetyltransferase (NAT)  enzymes. It occurs as a co-translational and post-translational modification of  proteins, for example, histones, STAT, and microtubules. Acetylation  modification regulates protein conformation, and dysfunction of this  modification has been implied in many diseases, including cancer. This type of  acetylation is co-translational, in that N-terminus is acetylated on growing  polypeptide chains that are still attached to the ribosome. While 80-90% of  eukaryotic proteins are acetylated in this manner, the exact biological  significance is still unclear.

N-terminal  Acetylation

N-acetylation, or the transfer of an acetyl  group to nitrogen, occurs in almost all eukaryotic proteins through both  irreversible and reversible mechanisms. N-terminal acetylation requires the  cleavage of the N-terminal methionine by methionine aminopeptidase (MAP) before  replacing the amino acid with an acetyl group from acetyl-CoA by  N-acetyltransferase (NAT) enzymes. This type of acetylation is  co-translational, in that N-terminus is acetylated on growing polypeptide  chains that are still attached to the ribosome. While 80-90% of eukaryotic  proteins are acetylated in this manner, the exact biological significance is  still unclear.

Lysine  Acetylation - Regulation of Histone

Acetylation at the ε-NH2 of lysine (termed  lysine acetylation) on histone N-termini is a common method of regulating gene  transcription. Histone acetylation is a reversible event that reduces  chromosomal condensation to promote transcription, and the acetylation of these  lysine residues is regulated by transcription factors that contain histone  acetyletransferase (HAT) activity. While transcription factors with HAT  activity act as transcription co-activators, histone deacetylase (HDAC) enzymes  are co-repressors that reverse the effects of acetylation by reducing the level  of lysine acetylation and increasing chromosomal condensation. While  acetylation was first detected in histones, cytoplasmic proteins have been  reported to also be acetylated, and therefore acetylation seems to play a  greater role in cell biology than simply transcriptional regulation.  Furthermore, crosstalk between acetylation and other post-translational  modifications, including phosphorylation, ubiquitination and methylation, can modify the biological function of the acetylated  protein.

N-acetylation

Creative Proteomics has established a  highly sensitive HPLC-MS/MS platform that can analyze acetylation in multiple  samples and in both eukaryotic and prokaryotic organisms. In addition, we have  optimized our protocol to enable more fast and sensitive site mapping service  for acetylation analysis.

Workflow  of our Acetylation analysis service:

Technology platform:

Creative Proteomics also provide the following bioinformatics services in Protein Post-translational Modification Analysis:
 Functional annotation and enrichment analysis
 Clustering analysis
 Network analysis
 Statistical analysis
 Proteomic analysis of post-translational modifications

Please feel free to Contact Us to discuss your projects. We hope you will find that we can meet your research needs.

Ordering Procedure:

Ordering Procedure


* For Research Use Only. Not for use in diagnostic procedures.
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