Protein Acetylation Assay

      Creative BioMart offers comprehensive Protein Acetylation Assay Services , combining cutting-edge technologies with deep expertise in post-translational modification research. Our histone acetylation assays and site identification services deliver fast, sensitive, and consistent results, empowering researchers to study protein regulation, epigenetic modifications, and disease mechanisms. Using advanced platforms, we provide assays capable of detecting global and site-specific histone acetylation in a wide range of mammalian samples, including fresh or frozen tissues, as well as cultured suspension and adherent cells. With Creative BioMart, clients benefit from a reliable partner offering convenience, precision, and unmatched assay performance.

      Tubulin protein acetylation structure

      Protein Acetylation: Background and Biological Significance

      Protein acetylation, particularly histone acetylation, plays a central role in regulating gene expression, chromatin structure, and protein function. Abnormal acetylation patterns have been linked to cancer, neurodegenerative disorders, and other complex diseases, making acetylation studies crucial in both basic and translational research.

      Histone acetylation and deacetylation mechanism

      Figure 1. Schematic representation of histone acetylation and deacetylation process. (Miziak et al., 2024)

      Histone H3 acetylation linked to cancer

      Figure 2. Histone H3 acetylation in cancer. (A) Examples of major histone H3 modifications by acetylation that promote (left panel) or inhibit (right panel) tumor growth. (B) Examples of the major lysines (K) acetylated in histone H3 across different cancer types that may serve as cancer biomarkers. HNCs—head and neck cancers. (Miziak et al., 2024)

      Traditional acetylation detection methods often face challenges such as poor sensitivity, low reproducibility, and complex workflows. Creative BioMart addresses these issues by offering streamlined, highly sensitive, and safer acetylation assays optimized for accuracy and reproducibility across diverse experimental systems.

      Protein Acetylation Assay Services

      Creative BioMart provides a full suite of Protein Acetylation Assay services, including:

      Global histone acetylation assays by Janczura et al., 2018

      Global Histone Acetylation Assays

      Fast and reliable quantification of acetylation on histone H3 and H4.

      Diagram of histone acetylation process

      Site-Specific Acetylation Detection

      Identification of acetylation at individual lysine residues.

      STAT3 protein structure with acetylation residue

      Custom Protein Acetylation Assays

      Available for non-histone proteins and specialized research needs.

      Service Workflow

      Workflow of protein acetylation assay service

      Key Features

      • Sample Flexibility: Compatible with fresh/frozen tissues, adherent cells, and suspension cells.
      • High-Sensitivity Kits: Detection of acetylation with extremely low detection limits.
      • Safety & Reliability: Methods optimized for minimal background noise and improved consistency.
      • Broad Applications: Ideal for epigenetics research, oncology studies, drug discovery, and biomarker development.

      Why Choose Our Acetylation Analysis Expertise

      Fast and Efficient: High-throughput compatible assays with quick turnaround times.
      Exceptional Sensitivity: Detects acetylation at extremely low abundance.
      Comprehensive Coverage: Global and site-specific histone acetylation analysis.
      Reliable Controls: Built-in assay controls ensure accurate quantification.
      Flexibility Across Samples: Works with multiple tissue and cell sample types.
      Trusted Expertise: Backed by years of experience in acetylation biology and assay development.

      Case Studies and Real-World Applications

         

      Case 1: Lactic acid drives histone acetylation and immune regulation

      Shi et al., 2024. doi:10.1016/j.celrep.2024.113746

      Lactic acid plays a pivotal role in shaping macrophage responses by modulating histone acetylation. Acting as a fuel source, it promotes histone H3K27 acetylation, which enables expression of immunosuppressive genes such as Nr4a1 and suppresses pro-inflammatory transcription. This effect persists as a form of “trained immunosuppression,” where pre-exposure induces tolerance to inflammatory stimuli. Mechanistically, lactic acid contributes to acetyl-CoA production via ATP-citrate lyase, fueling histone acetylation. Comparisons with HDAC inhibitors confirmed its capacity to restore H3K27 acetylation and repress inflammation. These findings highlight lactic acid as a key regulator of chromatin remodeling and long-term immune homeostasis.

      Lactic acid regulation of histone H3K27 acetylation in macrophages

      Figure 4. Lysine acetylation status is analyzed by using SDS-PAGE and Western blotting. Protein samples were collected from different tissues: 1. Suspension cells, 2. Endosperm (5 days after anthesis), 3. Flower, and 4. Leaf. (Nallamilli et al., 2014)

      Case 2: Lysine acetylation in rice proteins

      Nallamilli et al., 2014. doi:10.1371/journal.pone.0089283

      Lysine acetylation is a dynamic and reversible protein modification controlled by acetyltransferases and deacetylases. While global acetylation has been extensively studied in human cells, E. coli., and dicot plants, knowledge in monocots, especially cereals, remains limited. Using high-throughput mass spectrometry, researchers identified 60 lysine-acetylated sites on 44 rice ( Oryza sativa ) proteins spanning diverse biological functions. Immunoblot validation confirmed widespread non-histone acetylation. Analysis revealed conserved amino acid preferences around acetylation sites, and gene ontology showed acetylation occurs in cytoplasmic, chloroplast, and mitochondrial proteins. These findings indicate lysine acetylation serves as a broad regulatory mechanism in both histone and non-histone proteins.

      Lysine acetylation profile in rice proteins

      Figure 3. Phosphorylation of histone H2AX by different VRK1 pathogenic variant proteins performed by in vitro radioactive kinase assay. The graph shows the ratio of phosphorylated and non-phosphorylated substrates for each protein. (Martín-Doncel et al., 2019)

      Client Success Stories with Acetylation Assays

      FAQs About Protein Acetylation Services

      • Q: What types of protein acetylation can you measure?

        A: We provide both global and site-specific acetylation assays, covering histone H3 and H4 as well as custom targets on non-histone proteins. Our assays quantify acetylation levels at individual lysine residues or across the entire protein.
      • Q: What types of samples are compatible with your assays?

        A: Our assays work with a wide range of samples, including fresh or frozen tissues, cultured adherent cells, and suspension cells, making them highly versatile for both in vitro and ex vivo studies.
      • Q: How sensitive and reliable are your assays?

        A: Our methods offer extremely low detection limits, high reproducibility, and built-in controls for accurate quantification, ensuring consistent and trustworthy results across experiments.
      • Q: Can you support custom acetylation studies?

        A: Yes. We provide custom assay development and site identification services for specialized research needs, including non-histone proteins or specific acetylation sites, tailored to your project goals.
      • Q: How fast can I expect results?

        A: Our streamlined platforms and optimized workflows allow for rapid, high-throughput processing without compromising accuracy, giving researchers timely access to critical data.
      • Q: Why choose Creative BioMart over other providers?

        A: We combine industry-leading expertise, highly sensitive assays, broad sample compatibility, and reliable controls to deliver precise, reproducible, and efficient results. Our experience and technology ensure your acetylation studies are performed with confidence and scientific rigor.

      Resources

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      References:

      1. Miziak P, Baran M, Borkiewicz L, Trombik T, Stepulak A. Acetylation of histone H3 in cancer progression and prognosis. IJMS . 2024;25(20):10982. doi:10.3390/ijms252010982
      2. Nallamilli BRR, Edelmann MJ, Zhong X, et al. Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice ( Oryza sativa ). Soberón M, ed. PLoS ONE. 2014;9(2):e89283. doi:10.1371/journal.pone.0089283
      3. Janczura KJ, Volmar CH, Wahlestedt C. Purification of h3 and h4 histone proteins and the quantification of acetylated histone marks in cells and brain tissue. JoVE. 2018;(141):58648. doi:10.3791/58648
      4. Shi W, Cassmann TJ, Bhagwate AV, Hitosugi T, Ip WKE. Lactic acid induces transcriptional repression of macrophage inflammatory response via histone acetylation. Cell Reports. 2024;43(2):113746. doi:10.1016/j.celrep.2024.113746

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