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O-Glycoprotease is a specific endoprotease for O-glycoproteins, capable of catalyzing the hydrolysis of peptide bonds directly adjacent to O-glycan structures in natural mucin-type O-glycosylated proteins. The sequence of O-Glycoprotease is derived from Akkermansia muciniphila, and it is recombinantly expressed in E. coli with a C-terminal 6×His tag. This enzyme maintains high activity within a pH range of 5.5 to 7.5, is resistant to 1 M NaCl, but is highly sensitive to EDTA (0.5 mM EDTA) and can be inhibited by Zn2+.
| Pack Size | Price | USA Warehouse | Global Warehouse | Quantity |
|---|---|---|---|---|
| 10 mg | Inquiry | Inquiry | Inquiry | |
| 50 mg | Inquiry | Inquiry | Inquiry |
| Description | O-Glycoprotease is a specific endoprotease for O-glycoproteins, capable of catalyzing the hydrolysis of peptide bonds directly adjacent to O-glycan structures in natural mucin-type O-glycosylated proteins. The sequence of O-Glycoprotease is derived from Akkermansia muciniphila, and it is recombinantly expressed in E. coli with a C-terminal 6×His tag. This enzyme maintains high activity within a pH range of 5.5 to 7.5, is resistant to 1 M NaCl, but is highly sensitive to EDTA (0.5 mM EDTA) and can be inhibited by Zn2+. |
| Storage | Powder: -20°C for 3 years | In solvent: -80°C for 1 year |
Dissolve 2 mg of the compound in 100 μL DMSO
to obtain a stock solution at a concentration of 20 mg/mL . If the required concentration exceeds the compound's known solubility, please contact us for technical support before proceeding.
1) Add 100 μL of the DMSO
stock solution to 400 μL PEG300
and mix thoroughly until the solution becomes clear.
2) Add 50 μL Tween 80 and mix well until fully clarified.
3) Add 450 μL Saline,PBS or ddH2O
and mix thoroughly until a homogeneous solution is obtained.
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