Fusion DNA polymerase (Pfu-Sso7d) 100 u.a.

Fusion DNA polymerase is a recombinant polypeptide consisting of a fusion of the thermostable DNA polymerase of Pyrococcus furiosus (Pfu) and the DNA binding protein of the thermophilic archaea species Sulfolobus solfataricus (Sso7d). The Sso7d protein binds to the minor groove of double-stranded DNA and further stabilizes the polymerase-template complex. Due to this, Fusion DNA polymerase has increased processivity, synthesis accuracy, fragment amplification rate, and increased resistance to PCR inhibitors compared to native Pfu DNA polymerase [1]. Fusion DNA polymerase has 5'→3' polymerase activity, 3'→5' exonuclease activity and synthesizes blunt-ended products.
Fusion DNA polymerase is a good choice for routine cloning and can be used to generate long or complex amplicons by PCR.
Examples of using Fusion DNA polymerase are presented at the end of the description.
Fusion DNA polymerase was isolated from an E. coli strain containing a plasmid with a cloned DNA fragment consisting of the fusion genes of the thermostable DNA polymerase of Pyrococcus furiosus (Pfu) and the DNA-binding protein of Sulfolobus solfataricus (Sso7d).
One unit of activity corresponds to the amount of enzyme required to incorporate 10 nmol of dNTP into the acid-insoluble DNA fraction in 30 min at 74°C.