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Cat. No.: CAS9SG-500 (for 500pmol)

Cat. No.: CAS9SG-2500 (for 2500pmol)

Description

SpCas9‑sfGFP nuclease is a fusion protein combining Streptococcus pyogenes Cas9 (SpCas9) with superfolder GFP (sfGFP), integrating genome‑editing capability with robust fluorescence visualization. sfGFP is an engineered variant of traditional GFP, incorporating specific amino acid mutations that significantly enhance folding efficiency and structural stability. These improvements allow sfGFP to maintain strong fluorescence even when expressed as a fusion protein, overcoming the misfolding and fluorescence quenching issues commonly observed with wild‑type GFP.

The fusion protein is typically constructed by linking sfGFP to either the N‑terminus or C‑terminus of SpCas9 via a flexible peptide linker. Studies have shown that sfGFP fusion does not interfere with the nuclease activity of SpCas9. The protein retains its ability to recognize the NGG PAM sequence and, guided by sgRNA, introduces precise double‑strand breaks at the target DNA site. Meanwhile, the sfGFP fluorescence provides a direct and real‑time visualization tool for tracking Cas9 behavior.

SpCas9‑sfGFP enables real‑time monitoring of Cas9 spatiotemporal dynamics in living cells. Using fluorescence microscopy, researchers can directly observe cellular uptake efficiency, cytoplasmic trafficking, nuclear import, and binding/dissociation kinetics at chromatin target sites. Combined with flow cytometry or high‑content imaging, the fusion protein also allows quantitative evaluation of delivery efficiency across different delivery systems (e.g., lipid nanoparticles, viral vectors, nanomaterials), supporting the optimization of gene‑therapy vector design. Additionally, SpCas9‑sfGFP can be used for screening small‑molecule modulators of Cas9 activity or studying binding dynamics at specific genomic regions, further expanding the applications of CRISPR technology in basic research and translational medicine.

Potential Research Applications