SAN HQ 2.0
High activity at high salt conditions
High purity (≥ 99%)
Active at low temperatures
No protease detected
Table 1. Due to its high ioselectric point, SAN HQ 2.0 binds strongly to cation exchange media, even at elevated pH and salt concentrations where few other proteins show binding. SAN HQ 2.0 typically does not bind to anion exchange or IMAC media.
- Source: Recombinantly produced in Pichia pastoris
- Molecular weight: 26 kDa
- Protein purity: > 99% by SDS-PAGE analysis
- Isoelectric point: 9.55
- Unit definition: One unit is defined as the amount of enzyme that causes a ΔA260 = 1.0 in 30 minutes at 37°C in 25 mM Tris-HCI pH 8.5 (@25°C), 5 mM MgCl2, 500 mM NaCl, and 50 μg/ml calf thymus DNA.
- Specificity: Nonspecific endonuclease cleaving single- and double stranded DNA and RNA. The enzyme degrades DNA vs RNA in a 10:1 ratio.
- Working ranges:
- Temperature: 5 – 40°C, optimal: ~35°C
- Salt concentration (NaCl / KCl): 150 - 900 mM, optimal: 400 - 650 mM
- Mg2+: >1 mM is required for activity, optimal 5 - 50 mM
- pH: 7.3 – 10.0, optimal 8.2 - 9.2
Note: The working range is defined as ~20% of activity and optimal range is ~80% of activity.
- Tolerance to typical buffer additive:
- Triton X-100: No reduction in activity (tested up to 15%)