Dibasic endoprotease, also known as Kex2 protease or YSCF protease, is responsible for processing the precursors of killer toxin and α-factor in yeast. It is a calcium-dependent serine protease that specifically recognizes and cleaves peptide bonds at the carboxyl terminus of dibasic amino acid pairs such as Arg-Arg and Lys-Arg. Unlike trypsin, Kex2 cannot recognize or cleave peptide bonds at the carboxyl terminus of single basic amino acids (i.e., arginine or lysine). The activity of Kex2 protease is not inhibited by conventional serine protease inhibitors such as aprotinin, PMSF, or TPCK.
Yeasen recombinant Kex2 protease is expressed in Pichia pastoris, contains no animal-derived components, and is free from animal-derived viral contamination. It possesses the same enzymatic specificity as the native Saccharomyces cerevisiae Kex2 protease. The optimal pH for activity is pH 9.0, and the stable storage pH range is 5.0-6.0.
This Yeasen recombinant Kex2 protease is supplied in liquid form at a concentration of 1 mg/mL, ready for immediate use. Additionally, Yeasen also offers recombinant Kex2 protease in lyophilized powder form (Cat#20418ES), which can be stored at 2-8°C.
Product Information
|
Catalog No. |
Size |
|
20385ES60/80/90 |
100 μg / 1 mg / 10 mg |
Specifications
|
Source |
Recombinant expression in Pichia pastoris |
|
Molecular Weight |
Theoretical value 67.0 ± 6.7 kDa |
|
Appearance |
Sterile liquid |
|
Concentration |
1 mg/mL |
|
Storage Buffer |
10 mM NaAc-HAc, 50% glycerol, pH 5.2 |
|
Specific activity |
≥ 10.0 units/mg protein |
|
Purity |
≥ 95% |
|
Activity Definition |
At 25°C in a 3 mL reaction system containing 50 mM Tris-HCl and 2 mM CaCl₂, pH 8.0, one unit (Unit) of enzyme activity is defined as the amount of enzyme that catalyzes the release of 1 μmol of 4-nitroaniline from the substrate Boc-QRR-pNA per minute. |
Properties
|
Source |
Pichia pastoris recombinant expression |
|
Molecular Weight |
Theoretical 67.0 ± 6.7 kDa |
|
Appearance |
Sterile liquid |
|
Concentration |
1 mg/mL |
|
Storage Buffer |
10 mM NaAc-HAc, 50% glycerol, pH 5.2 |
|
Specific Activity |
≥10.0 units/mg pro |
|
Purity |
≥95% |
|
Activity Definition |
At 25°C, in a 3 mL reaction system containing 50 mM Tris-HCl, 2 mM CaCl₂, pH 8.0, one unit (U) is defined as the amount of enzyme that catalyzes the release of 1 μmol of 4-nitroaniline from the substrate Boc-QRR-pNA per minute |
Application
Usage Instructions (Application Example):
1. Reaction System:
|
Component |
Amount |
|
Fusion Protein |
5 mg |
|
Kex2 Enzyme |
5-100 μg (Recommended ratio: protease to fusion protein mass ratio 1:50 to 1:1000) |
|
Buffer System (50 mM Tris-HCl, 2 mM CaCl₂, pH 8.0) |
Up to 100 μL |
2. Reaction Conditions: Mix thoroughly, incubate at 37°C for 10 min.
[Note]: 50 mM Tris-HCl, 2 mM CaCl₂, pH 8.0 can be used as the reaction diluent; the reaction volume can be scaled up according to the amount of substrate.
Storage
FAQ
Citations
Documents
| Brochure |
|---|
| Industrial_Production_Solutions_for_Tirzepatide_and_Semaglutide.pdf |
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