108 articles
Spin trapping
Spin trapping is a technique, introduced by Edward G. Janzen and Barry J. Blackburn in 1968, that converts short-lived radicals into stable nitroxide adducts detectable by EPR spectroscopy.
Stable isotope labeling by amino acids in cell culture
Stable isotope labeling by amino acids in cell culture (SILAC) is a metabolic labeling method for quantitative proteomics, reported by Shao-En Ong and colleagues in 2002.
Staining
Staining: use of dyes, fluorochromes, and metal-salt reactions to add contrast to colorless biological specimens. Covers ionic and covalent binding mechanisms, H&E and special stains, fluorescence, Biological Stain Commission certification, and digital deep-learning virtual staining.
Strand displacement amplification
Strand displacement amplification (SDA) is an isothermal DNA amplification method, reported in 1992, that uses a nicking enzyme and a strand-displacing polymerase to copy a target sequence exponentially at a single constant temperature.
SWATH-MS
SWATH-MS is a data-independent mass spectrometry method, reported in 2012, that fragments all ions in sequential windows to quantify peptides and proteins in complex samples.
SYBR Green I
SYBR Green I is an unsymmetrical cyanine fluorescent dye that binds double-stranded DNA, widely used for detecting and quantifying DNA in gels and real-time PCR.
Tandem affinity purification
Tandem affinity purification (TAP) is a protein purification method that isolates native protein complexes through two sequential affinity tags, first reported by Rigaut and colleagues in 1999.
Tandem mass tag labeling
Tandem mass tag (TMT) labeling is a proteomics method in which peptides from different samples are tagged with isobaric labels, so one mass spectrometry run quantifies proteins across all samples.
Terminal amine isotopic labeling of substrates
Terminal amine isotopic labeling of substrates (TAILS) is a proteomics method, introduced in 2010, that identifies protease substrates by isotopic dimethylation and negative selection of N-terminal peptides.
Thermal proteome profiling
Thermal proteome profiling (TPP) is a mass spectrometry method that measures the thermal stability of thousands of proteins to detect drug-target engagement in living cells.
Thioflavin T
Thioflavin T is a benzothiazole cationic dye that fluoresces strongly when bound to amyloid fibrils, the most widely used probe for detecting protein aggregation in vitro.
TMTpro
TMTpro is a family of amine-reactive isobaric tandem mass tag reagents sold by Thermo Fisher Scientific that expands multiplexed proteome quantification to 16 and 18 samples per run.
Top-down proteomics
Top-down proteomics is a mass spectrometry approach that analyzes intact proteins without prior digestion, characterizing each protein's sequence variants and post-translational modifications at the proteoform level, in contrast to bottom-up shotgun proteomics.
Tris
Tris (tris(hydroxymethyl)aminomethane, THAM, tromethamine) is an organic buffer with pKa about 8.1, used at pH 7-9 in biochemistry, as the drug THAM for acidosis, and as the seawater pH standard.
Tris(2-carboxyethyl)phosphine
Tris(2-carboxyethyl)phosphine (TCEP) is an odorless, water-soluble tertiary phosphine that cleaves disulfide bonds in proteins and oligonucleotides, widely used in place of dithiothreitol because it resists air oxidation.
Tryptic digestion
Tryptic digestion, also called trypsin digestion, is a proteomics method in which the enzyme trypsin cleaves proteins after lysine and arginine into peptides for mass spectrometry, accounting for 96% of deposited peptide identifications.
Tunable resistive pulse sensing
Tunable resistive pulse sensing (TRPS) is a single-particle technique applying the Coulter principle through a tunable nanopore to measure nanoparticle size, concentration, and zeta potential, widely used for extracellular vesicles.
Universal indicator
Universal indicator is a pH indicator solution of several dyes that shows a distinct color for each pH level across the full range, typically 1 to 14.