Cleavage and Tag Control Protein

• Species: artificial
• Tags: Twin-Strep, HA, T7, Avi, FLAG, and His-tag; N-terminal MBP and C-terminal sfGFP fusion

• Expression Host: E. coli
  
• Formulation: PBS; pH 7.4
  
• Format:
  Liquid: stored and shipped at -80 °C.
  Lyophilized: stored at -80 °C and shipped at ambient temperature. We recommend reconstituting the protein in ddH2O. In case of 10 µg, add 11 µl ddH2O.
• Purity: > 99 % (measured by densitometry of Coomassie stained gel, see below)
  

The Cleavage and Tag Control Protein is a versatile protein consisting of various cleavage sites for proteases including TEV, Enterokinase, Thrombin, Factor Xa and PreScission™ Protease cleavage results in generation of two or three fragments that have significantly reduced molecular weights, which are as follows:
- TEV cleavage: 42.8 kDa and 47.7 kDa
- Enterokinase: 43.5 kDa, 20.1 kDa and 26.9 kDa
- Thrombin: 43.9 kDa and 46.6 kDa
- Factor Xa: 44.3 kDa and 46.2 kDa
- PreScission™: 45.3 kDa and 45.3 kDa
Moreover, the 90.5 kDa fusion protein is equipped with multiple tags such as Twin-Strep-, HA-, FLAG-, and His-tag, for instance, that may serve as positive control performing specific Western Blot analyses or any functional assay. Since the protein is fused to GFP, it is additionally applicable as fluorescence control. Thus, the Cleavage and Tag Control Protein provides an excellent tool to monitor protease cleavage reactions and specific Western Blot analyses as well as fluorescence experiments.

SDS-PAGE/Coll. Coomassie	Histogram of marked lane in gel picture

Test Cleavage	Description of Test Cleavage
Test Cleavage	Description for Test Cleavage

Download Product Information for Cleavage and Tag Control Protein, liquid

Download Product Information for Cleavage and Tag Control Protein, lyophilized