MALDI TOF Protein Analysis Service
MALDI TOF Protein Analysis Service is a powerful technique that leverages Matrix-Assisted Laser Desorption/Ionization Time-of-Flight (MALDI-TOF) mass spectrometry for identifying and characterizing proteins based on their mass-to-charge ratio. In the MALDI TOF protein analysis method, proteins are mixed with a matrix, then ionized by a laser, which results in charged protein ions. These ions are accelerated in a time-of-flight analyzer, where their travel time to the detector is measured. The time it takes for the ions to reach the detector is inversely related to their mass, enabling precise identification of the protein's molecular weight.
Figure 1. MALDI-TOF MS Methodology
The MALDI TOF Protein Analysis Service provides rapid, high-throughput protein identification and molecular weight determination. The MALDI TOF Protein Analysis Service is widely used for applications such as protein fingerprinting, biomarker discovery, and quality control in pharmaceutical and biotechnology industries. Additionally, the MALDI TOF Protein Analysis Service is especially useful in characterizing complex protein mixtures, identifying protein modifications like glycosylation, and validating recombinant proteins.
Services at MtoZ Biolabs
MtoZ Biolabs offers MALDI TOF Protein Analysis Service which ensures high accuracy and reliability with advanced instrumentation and expert analysis. Our MALDI TOF Protein Analysis Service enables researchers to gain detailed insights into protein identity, structure, and functionality, providing valuable support for research, development, and quality control.
Figure 2. General Workflow of Cancer Diagnostic via MALDI-TOF MS for Proteome/Peptidome
Service Advantages
1. High Sensitivity and Accuracy: The MALDI TOF Protein Analysis Service offers exceptional sensitivity and accuracy in protein identification and molecular weight determination, ensuring precise results even with low-abundance proteins in complex samples.
2. Rapid and High-Throughput Analysis: The MALDI TOF Protein Analysis Service enables fast, high-throughput analysis, providing timely results for large-scale proteomics studies. The ability to process multiple samples simultaneously accelerates research and development timelines.
3. One-Time-Charge: Our pricing is transparent, no hidden fees or additional costs.
Applications
1. Intact Mass Determination
The MALDI TOF Protein Analysis Service efficiently determines the intact mass of proteins, offering critical information about their size, structure, and potential heterogeneity.
2. Peptide Mass Fingerprinting
This technique generates peptide mass fingerprints, enabling the identification of proteins by matching peptide masses with protein databases, making it an essential tool in proteomics research.
3. Quality Control in Biotechnology and Pharmaceuticals
MALDI TOF is extensively used for quality control in biotechnology and pharmaceutical industries to verify the identity and purity of recombinant proteins and to ensure consistency in production processes.
4. Glycosylation and Post-Translational Modification Analysis
The MALDI TOF Protein Analysis Service helps detect and characterize protein modifications such as glycosylation, phosphorylation, and acetylation, providing insights into protein functionality and regulation.
5. Protein Complex Analysis
MALDI TOF allows for the study of protein complexes, offering a deeper understanding of protein interactions and their roles in cellular processes.
Sample Results
Figure 3. MALDI-TOF Mass Spectra Obtained of Protein Extracts from 4 Different Commercial Quinoa Grains
Deliverables
1. Comprehensive Experimental Details
2. Materials, Instruments, and Methods
3. Total Ion Chromatogram & Quality Control Assessment (project-dependent)
4. Data Analysis, Preprocessing, and Estimation (project-dependent)
5. Bioinformatics Analysis
6. Raw Data Files
For more information about our MALDI TOF Protein Analysis Service, please contact us.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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