Custom Premix Selecting "Custom Premix" option means that all of the beads you have chosen will be premixed in manufacturing before the kit is sent to you.
The Factor Xa Cleavage Capture Kit is designed for highly specific cleavage of fusion proteins followed by convenient affinity-based capture and removal of Factor Xa. After cleavage of the target protein, Factor Xa is removed with greater than 99% efficiency from the reaction by affinity capture on Xarrest™ Agarose. Following capture of Factor Xa, the agarose is removed by spin-filtration. No buffer changes are necessary because the same buffer conditions are used for both cleavage and capture. The kit includes a Cleavage Control Protein for conducting control digests in parallel with experimental samples, or to test cleavage under customized buffer conditions. The 49 kDa Xa Cleavage Control Protein is cleaved into two proteolytic fragments of 32 kDa and 17 kDa, which are easily visualized by standard SDS-PAGE followed by Coomassie blue staining. The Xa Cleavage Control Protein also features an amino terminal S•Tag™ sequence enabling sensitive detection of the 17 kDa proteolytic product with Western Blot reagents..
Specific Activity: ≥150 IU/ug
One IU is defined as the amount of enzyme that will release 1 µmole of p-nitroaniline per minute using methanesulfonyl-D-leucyl-glycyl-arginyl-paranitroanilide at 37°C, pH 8.4.
One µg of enzyme cleaves 50 µg Cleavage Control Protein to >95% completion in 16 hr at 25°C in a buffer containing 50 mM Tris-HCl pH 8.0, 100 mM NaCl, and 5 mM CaCl2.
Catalogue Number
69037
Brand Family
Novagen®
References
Product Information
•
100 µg
Restriction Grade Factor Xa
•
2 ml
Factor Xa Dilution/Storage Buffer
•
5 ml
10X Factor Xa Cleavage/Capture Buffer
•
2 × 2.5 ml
Xarrest™ Agarose
•
10 µg
Xa Cleavage Control Protein
•
pkg/10
Spin Filters, 2 ml capacity
Applications
Biological Information
Biological activity
One microgram of enzyme cleaves 50 µg Xa Cleavage Control Protein to >95% completion in 16 hours at 25°C in a buffer containing 50 mM Tris-HCl pH 8.0, 100 mM NaCl, and 5 mM CaCl₂.
Domenico Sanfelice, et al. (2004) Letter to the editor: resonance assignment and secondary structire of the La motif. Journal of Biomolecular NMR29, 449-450.