Protein 2-Hydroxyisobutyrylation Analysis

Post-translational modifications (PTMs) involve chemical changes to proteins during or after their synthesis, playing crucial roles in cellular processes such as differentiation, degradation, signal transduction, gene expression regulation, and protein-protein interactions. 2-Hydroxyisobutyrylation (2HIB), a novel PTM first identified in histones, involves the covalent attachment of a 2-hydroxyisobutyryl group to lysine residues in proteins. This modification significantly impacts gene expression, metabolic pathways, and signal transduction.

MtoZ Biolabs offers a dedicated Protein 2-Hydroxyisobutyrylation Analysis that enables researchers to accurately detect, enrich, and characterize 2-hydroxyisobutyrylated proteins across diverse biological samples. By integrating optimized enrichment strategies with high-resolution LC-MS/MS, our platform supports both targeted analysis of specific proteins and large-scale profiling of 2-hydroxyisobutyrylation events.

This service helps overcome challenges such as low-abundance modification detection and complex sample backgrounds, ensuring reliable identification and quantitative evaluation. MtoZ Biolabs provides robust analytical support for studies exploring regulatory mechanisms, protein function, and broader biological implications of 2-hydroxyisobutyrylation.

Services at MtoZ Biolabs

1. Target protein 2-hydroxyisobutyrylation analysis

MtoZ Biolabs provides Target Protein 2-Hydroxyisobutyrylation Analysis focusing on the identification and verification of 2-hydroxyisobutyrylation (Khib) modifications on specific proteins. By combining immunoprecipitation with high-resolution mass spectrometry (LC-MS/MS), this service precisely locates modification sites, evaluates modification abundance, and analyzes the potential impact on protein structure and function. It is suitable for mechanistic studies and functional validation, helping researchers confirm the post-translational modification status of key regulatory proteins.

2. 2-hydroxyisobutyrylation proteomics

MtoZ Biolabs offers 2-Hydroxyisobutyrylation Proteomics based on high-sensitivity mass spectrometry and specific enrichment strategies to comprehensively analyze Khib modification profiles at the cellular or tissue level. This service enables large-scale identification and quantification of thousands of Khib-modified proteins and sites. Combined with bioinformatics analysis, it reveals regulatory networks involved in metabolism, signal transduction, and disease processes, providing global data support for downstream target discovery and functional research.

If you are interested in our protein 2-hydroxyisobutyrylation analysis service, please feel free to contact us. We are dedicated to providing you with the best service.

Analysis Workflow

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Service Advantages

1. Advance Analysis Platform: Mtoz Biolabs established an advanced protein 2-hydroxyisobutyrylation analysis analysis platform, guaranteeing reliable, fast, and highly accurate analysis service.

2. One-Time Charge: Our pricing is transparent, with no hidden fees or additional costs.

3. High-Data-Quality: Deep data coverage with strict data quality control. AI-powered bioinformatics platform integrate all protein 2-hydroxyisobutyrylation analysis data providing clients with acomprehensive data report.

4. Comprehensive Analysis: Both target protein 2-hydroxyisobutyrylation analysis and 2-hydroxyisobutyrylation proteomics can be conducted in MtoZ Biolabs.

Sample Submission Requirements

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1. If you are providing tissue samples, please ship them to us on dry ice.

2. If you are providing protein samples, standard tissue or cell lysis buffers can be used during protein extraction.

3. Sample transportation: Please ensure that samples are shipped with sufficient dry ice and choose the fastest possible shipping way to minimize the risk of sample degradation during transit.

4. Before proceeding with the formal experiment, we will test the samples you provide, and the formal analysis will begin once the samples pass the quality check.