Product nameThrombin cleavage kit
Abcam’s Thrombin cleavage kit (ab207000) efficiently removes tags from recombinant fusion proteins containing an accessible thrombin cleavage sequence.
Thrombin is a valuable biochemical tool due to its high proteolytic specificity. A thrombin cleavage site (e.g., Leu-Val-Pro-Arg-ll-Gly-Ser; where ll denotes the cleavage site) is widely incorporated within the linker region of fusion or affinity tagged recombinant proteins. After successful cleavage with thrombin, affinity tags or fused proteins can be separated from the target protein. Abcam's Thrombin cleavage kit provides an easy approach to test and optimize cleavage conditions of a target fusion or affinity-tagged protein containing a thrombin-specific cleavage site. The kit contains active thrombin enzyme sufficient to cleave up to 5 mg of the target protein. A 6x His-tagged protein containing the thrombin cleavage site is included as a cleavage control protein. Following cleavage of the target protein, thrombin can be removed by passing the reaction mix through a Heparin Sepharose® column.
Tested applicationsSuitable for: Purificationmore details
Storage instructionsStore at -20°C. Please refer to protocols.
Components 500 tests Cleavage Control Protein (Lyophilized) 1 vial Thrombin Cleavage Buffer 1 x 25ml Thrombin Dilution Buffer 1 x 1ml Thrombin Enzyme 1 x 500µl
Our Abpromise guarantee covers the use of ab207000 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Purification||Use at an assay dependent concentration.|
SDS-PAGE analysis of thrombin cleavage using different amount of thrombin and ab207000: Cleavage of 10 μg of 6x His-tagged Cleavage Control Protein with different amounts (0.01-1 U/μL) of thrombin at room temperature for 18 hours.
SDS-PAGE analysis of thrombin cleavage at different time points using ab207000: Cleavage of 10 μg of 6x His-tagged Cleavage Control Protein.
ab207000 has not yet been referenced specifically in any publications.