Description
The PNGase F is a recombinant enzyme expressed in yeast, which can cleave high mannoses, heterozygotes, and complex oligosaccharide proteins linked by asparagine. The cleavage site of PNGase F is the amide bond between N-acetylglucosamine (GlcNAc) and asparagic acid residue on the inner side of the glycoprotein, and the aspartyl on the enzymatic hydrolysis protein is converted to aspartic acid. This product has a His tag and is often used for complete deglycosylation of antibodies and their related proteins.
Component
|
No. |
Name |
20415ES01 |
20415ES02 |
|
20415-A |
PNGase F |
15 KU |
75 KU |
|
20415-B1 |
Buffer 1（10×） |
150 μL |
750 μL |
|
20415-B2 |
Buffer 2（10×） |
300 μL |
1500 μL |
|
20415-B3 |
10% NP-40 |
300 μL |
1500 μL |
产品性质
|
Name |
PNGase F |
|
Source |
Expressed in Yeast |
|
Molecular weight |
36 kDa |
|
Specific activity |
750000 U/mL |
|
Buffer |
20 mM Tris-HCl pH 7.5, 50 mM NaCl, 5 mM EDTA,50% Glycerol |
|
Unit Definition |
One unit is defined as the amount of enzyme required to remove > 95% of the carbohydrate from 10 µg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10 µL. |
Shipping and Storage
The products are shipped with dry ice and can be stored at -15℃ ~ -25℃ for one year.