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Clostripain (EC 3.4.22.8, clostridiopeptidase B, clostridium histolyticum proteinase B, alpha-clostridipain, clostridiopeptidase, Endoproteinase Arg-C) is a proteinase that cleaves proteins on the carboxyl peptide bond of arginine. [1] [2] It was isolated from Clostridium histolyticum.
Hi-C uses high-throughput sequencing to find the nucleotide sequence of fragments [2] [22] and uses paired end sequencing, which retrieves a short sequence from each end of each ligated fragment. As such, for a given ligated fragment, the two sequences obtained should represent two different restriction fragments that were ligated together in ...
Between 2012 and 2015, several modifications to the Hi-C protocol have taken place, with 4-cutter digestion [10] or adapted deeper sequencing depth to obtain higher resolution. [8] [9] [11] The use of restriction endonucleases that cut more frequently, or DNaseI and Micrococcal nucleases also significantly increased the resolution of the method ...
Like typical next-generation sequencing experiments, single-cell sequencing protocols generally contain the following steps: isolation of a single cell, nucleic acid extraction and amplification, sequencing library preparation, sequencing, and bioinformatic data analysis. It is more challenging to perform single-cell sequencing than sequencing ...
Alternatively, uniform labeling with 13 C or 15 N can be used. Proteins from both cell populations are combined and analyzed together by mass spectrometry as pairs of chemically identical peptides of different stable-isotope composition can be differentiated in a mass spectrometer owing to their mass difference.
Pore-C is a relatively new method, so its applications have not yet been fully appreciated. [2] A strength of Pore-C over previous methods is its ability to detect interactions between more than two genomic loci. Such high-order interactions enable the study of cellular processes, such as gene expression regulation at a more system-level scale.
In 2012, the standard CAGE protocol was updated by Takahashi et al. [12] to cleave tags with EcoP15I and sequence them on the Illumina-Solexa platform. In 2013, Batut et al. [ 13 ] combined CAP trapper, template switching, and 5′-phosphate-dependent exonuclease digestion in RAMPAGE to maximize promoter specificity.
DNA fragments are first generated using ddRADseq protocol applied to fresh samples, and used as hybridization-capture probes to enrich shotgun libraries in the fragments of interest. This simple and cost-effective approach allows sequencing of orthologous loci even from highly degraded DNA samples, opening new avenues of research in the field ...