Cat. No. / ID: Not Applicable
Stoffel DNA Polymerase is a 62.7 kDa recombinant fragment of thermostable Taq DNA polymerase isolated from Thermus aquaticus. It is recommended for a wide range of applications that require DNA synthesis in extremely high temperatures.
The thermostability of Stoffel DNA Polymerase is about twice as high as the TaqNova DNA Polymerase. It requires a higher MgCl2 concentration level and lower ionic strength for optimum enzymatic activity. The vast magnesium optimum for Nova Stoffel DNA Polymerase reduces the need for magnesium optimization experiments. It increases the ease of multiplex PCR optimization which is the simultaneous amplification of multiple targets in the same reaction.
The increased thermal stability of the TaqNova Stoffel may lead to superior amplification of excessively GC-rich templates and templates with secondary structure by allowing denaturation temperatures as high as 98°C.
It is supplied with 20 mM Tris-HCl (pH 8.0 at 25°C), 100 mM KCl, 0.1 mM EDTA, 1 mM DTT, 0.5% (v/v) Nonidet P40, 0.5% (v/v) Tween 20, 50% (v/v) glycerol.
One unit is defined as the amount of enzyme required to incorporate 10 nmol of dNTPs to an insoluble DNA fraction in 30 minutes at 72°C in a 50 μL reaction.
Assay | Specification |
Protein Purity | ≥95% |
DNase contamination | None detected |
Stoffel fragment is encoded by a modified form of the Thermus aquaticus DNA polymerase gene, which has been inserted into an Escherichia coli host. The modified gene encodes a 540 amino acid fragment lacking the N-terminal 292 amino acid portion of the full-length TaqNova DNA Polymerase.
Quality Control
Protein purity is determined using Coomassie Blue detection assay by SDS-PAGE analysis resulting in ≥95% purity.
DNase contamination is evaluated through extensive PCR reactions.
This is used for applications such as: