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Integrated System for Rapid Proteomics Analyses Using Microfluidic Devices Coupled to Nanoelectrospray Mass Spectrometry
Time of Update: 2021-03-04
Enhancement of sample throughput is facilitated using an autosampler, a microfabricated device comprising a large (2.4-μL total volume) separation channel together with a low-dead-volume interface to nES mass spectrometry.
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Microbial Proteomics Using Mass Spectrometry
Time of Update: 2021-02-21
Proteomic analyses involve a series of intricate, interdependent steps involving approaches and technical issues that must be fully coordinated to obtain the optimal amount of required information about the test subject.
This fortunate occurrence creates an essential core of proteomic approaches and techniques that are consistently available for most studies, regardless of test subject.
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Use of Proteomic Tools in Microbial Engineering for Biofuel Production
Time of Update: 2021-02-20
Hierarchical clustering analysis revealed that over 70% of the 102 differentially expressed proteins in mutant Rh8 were either upregulated (e.g., chaperones and solvent formation related) or downregulated (e.g., amino acid metabolism and protein synthesis related) in both acidogenic and solventogenic phase, which, respectively, are only upregulated or downregulated in solventogenic phase in the wild-type strain.
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Proteome Analysis of Adenovirus Using Mass Spectrometry
Time of Update: 2021-01-26
For analysis of viral proteomes, an optimal protocol includes production of a highly purified virus that can be investigated with a high-resolving analytical method.
This method provides information on the chemical composition of the virus particle.
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Cancer screening using "sugar proteomics" the company completed a $34 million B round of financing
Time of Update: 2021-01-19
Recently, California-based InterVenn Biosciences announced the completion of a $34 million round of B financing, with Anzu Partners leading the way, and Genoa Ventures, Amplify Partners, True Ventures and others taking part.
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Characterization of the Plant Cell Wall Proteome Using High-Throughput Screens
Time of Update: 2021-01-13
Plant cell wall proteins play essential roles in many important biological processes, and yet there is still not a comprehensive catalogue of the cell wall proteome, or “secretome”.
The approaches are orthogonal and collectively provide a powerful suite of approaches to complement more commonly used strategies to isolate plant cell wall-associated proteins.
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Quantitative Proteomic Analysis of Mammalian Organisms Using Metabolically Labeled Tissues
Time of Update: 2020-12-30
Metabolic labeling of mammalian organisms with stable isotopes can be used to provide tissue-specific internal standards foruse in quantitative proteomic analyses.
This chapter will focus on the generation of the isotope-labeled tissues, the analysisof the sample using Multidimensional Protein Identification Technology, and the computational analysis of the mass spectrometricdata acquired.
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Computational Analysis of Quantitative Proteomics Data Using Stable Isotope Labeling
Time of Update: 2020-12-30
Although these methods have paved the way for quantitative proteomics, the analysis of these data is often the rate-limitingstep.
In this chapter, we have attempted to summarize several of the key steps necessaryfor an individual to automate the analysis of quantitative proteomics data.
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Use of Transcriptomic Data to Support Organelle Proteomic Analysis
Time of Update: 2020-12-29
Consequently,identification of genes whose expression correlates with organelle assembly leads to acandidate list that can be cross-checked with a preliminary organelle proteome.
Whenproteins are found in the proteome and the corresponding genes are found to have organelleassembly-correlated expression, this greatly increases our confidence that those proteinsare true components of the organelle and not contamination.
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The Use of a Quantitative Cysteinyl-Peptide Enrichment Technology for High-Throughput Quantitative Proteomics
Time of Update: 2020-12-27
A quantitative cysteinyl-peptide enrichment technology ( QC ET) can be employed to achievehigher efficiency, greater dynamic range, and higher throughput in quantitative proteomic studies based on the use of stableisotope-labeling techniques combined with high-resolution capillary or nano-scale liquid chromatography-mass spectrometry(LC-MS) measurements.
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Identification of SUMO-Conjugated Proteins and their SUMO Attachment Sites Using Proteomic Mass Spectrometry
Time of Update: 2020-12-24
One recent advance in the field of SUMO modification that has provided important insights into SUMO-mediated regulatory networks is the ability to use proteomic mass spectrometry to identify the substrates of SUMO modification as well as their sites of conjugation ( 1 – 10 ).
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Using the Global Proteome Machine for Protein Identification
Time of Update: 2020-12-19
The chapter describes the use of features of the Global Proteome Machine (GPM) interface that assist in making comprehensive assignments between spectra and sequences, including the detection of point mutations, posttranslational modifications, and experimental artifacts.
The use of this interface to validate results using the GPM Database is also described.
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A Novel Approach Using MALDI-TOF/TOF Mass Spectrometry and Prestructured Sample Supports
Time of Update: 2020-12-17
Mass spectrometry (MS)-based proteomic profiling and protein identification has become a powerful tool for the discovery of new disease biomarkers.
Here, we present a strategy using MALDI-TOF/TOF MS to analyze fractionated human serum samples for proteomic profiling and then identify serum peptides from these proteomic profiles.
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A Brief Summary of the Different Types of Mass Spectrometers Used in Proteomics
Time of Update: 2020-12-15
This wide diversity of instrumentation commercially available for mass spectrometry-based proteomics makes the choice of instrumentation sometimes difficult.
The choice of instruments depends on the biological problem and the proteomic strategy chosen for protein identification.
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Quantitative Proteomics of Mouse Brain and Specific Protein-Interaction Studies Using Stable Isotope Labeling
Time of Update: 2020-12-13
We describe a new method for quantitative tissue proteomics using culture-derived isotope tags (CDIT), which are cells grownin stable isotope-enriched medium and added to each tissue sample to provide internal standards.
After protein identificationby mass spectrometry (MS), each peak derived from tissue protein is quantified relative to the corresponding CDIT peak.
