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- CRISPR-Cas12a: Functional overview and applications
In this review, we aim to provide a mechanistic insight into the working mechanism of Cas12a, comparing it with Cas9, and eventually provide an overview of its current applications in genome editing and biotechnology applications
- Cas12a Cis-cleavage mediated lateral flow assay enables . . . - Nature
Here authors exploit CRISPR-Cas12a cis-cleavage to develop a multiplexed assay which includes a portable device incorporating multiplexed PCR, Cas12a cis-cleavage, and lateral flow detection
- EnGen Lba Cas12a (Cpf1) | NEB
EnGen Lba Cas12a (Cpf1) is a programmable DNA endonuclease guided by a single guide RNA (gRNA) Targeting requires a gRNA complementary to the target site as well as a 5' TTTN protospacer adjacent motif (PAM) on the DNA strand opposite the target sequence
- CRISPR-Cas12a target binding unleashes indiscriminate single . . . - Science
CRISPR-Cas12a (Cpf1) proteins are RNA-guided enzymes that bind and cut DNA as components of bacterial adaptive immune systems Like CRISPR-Cas9, Cas12a has been harnessed for genome editing on the basis of its ability to generate targeted, double-stranded DNA breaks
- Programmable RNA detection with CRISPR-Cas12a - Nature
Cas12a, a CRISPR-associated protein complex, has an inherent ability to cleave DNA substrates and is utilized in diagnostic tools to identify DNA molecules We demonstrate that multiple
- CRISPR Cas12a-Based Biosensing: Advances in Mechanisms and Applications . . .
CRISPR Cas12a-based detection systems can be regarded as a new type of biosensor, offering a practical and efficient approach for nucleic acid analysis in various diagnostic settings CRISPR Cas12a-based biosensors outperform conventional nucleic acid detection methods in terms of portability, simplicity, speed, and efficiency
- Cas12a: Definition, Applications, Industry Uses - Excedr
CRISPR-Cas12a (Cpf1) is a guide RNA-guided endonuclease that cleaves dsDNA using its RuvC domain It has three homologs, which include LbCas12a (from Lachnospiraceae bacterium), FnCas12a (from Francisella novicida), and AsCas12a (from Acidaminococcus sp )
- PAM-free hairpin target binding activates trans-cleavage activity of Cas12a
In this work, we found that a hairpin-structured substrate can activate the trans -cleavage activity of Cas12a without a PAM, and the parameters of the hairpin loop obviously affect the activity Cas12a exhibits sequence preference for proximal loops, preferring to recognize polyadenine hairpin loop activators
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