Part:BBa_K5412001
CAS12a_S14P_S60P
This mutant CAS12a protein features specific mutations where serine residues at positions 14 and 60 have been replaced with proline. These modifications are designed to explore their effects on the enzyme's structure, activity, and specificity in CRISPR applications. This is done to improve the stability of the CAS12a enzyme required for CF detection.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 1198
Illegal PstI site found at 1696
Illegal PstI site found at 3403 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 1198
Illegal PstI site found at 1696
Illegal PstI site found at 3403 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1371
Illegal BglII site found at 2775
Illegal BglII site found at 3120 - 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 1198
Illegal PstI site found at 1696
Illegal PstI site found at 3403 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 1198
Illegal PstI site found at 1696
Illegal PstI site found at 3403 - 1000COMPATIBLE WITH RFC[1000]
Plasmid Map of CAS12A mutant in Pet-23a+
References
Zhang, L., et al. (2021). Engineering CRISPR-Cas12a for enhanced target recognition and cleavage at elevated temperatures. Nature Communications, 12, 3908.
https://www.nature.com/articles/s41467-021-24117-z
Teng, F., et al. (2019). Crispr-Cas12a cleaves RNA in addition to DNA at elevated temperatures. Nature Communications, 10, 2162.
https://www.nature.com/articles/s41467-019-10148-6
Swarts, D. C., et al. (2017). DNA-guided DNA interference by a prokaryotic Argonaute. Nature, 507(7491), 258-261.
https://www.nature.com/articles/nature21049
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