计算溶液所需的质量、体积或浓度。
,适用于对基线干扰要求严格的色谱和分析工作流程。
2-8°C储存。低温运输 。请查阅批次 COA 获取详细规格。
SDS、COA、产品数据表及规格说明书均可下载。可通过批号查询获取批次 COA。
在色谱分析、有机合成和交叉偶联反应领域已被 0 篇同行评审文献引用。
Product Description
Endo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact.
Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However, for optimal results, denaturation of the glycoprotein is recommended.
Contents
60 µl aliquot of enzyme (0.3 U) in 10 mM sodium acetate 25mM NaCl, pH 4.5
Included with 20 µL and 60 µL pack sizes:
5x Reaction Buffer – 250 mM sodium acetate, pH 4.5
Molecular weight
32,000 daltons
Specific Activity
Defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured porcine fibrinogen in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved fibrinogen migrates faster).
Formulation
The enzyme is provided as a sterile-filtered solution in 10
mM sodium acetate, 25mM NaCl, pH 4.5
Specificity
Endo F2 cleaves Asparagine-linked biantennary and high mannose glycans (at a 40X reduced rate). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However for optimal results, denaturation of the glycoprotein is recommended.
Quality & Purity
Endo F2 is tested for contaminating protease as follows: 10 µg of denatured BSA is incubated at 37°C for 24 hours with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production host strain has been extensively tested and does not produce any detectable glycosidases.
Stability
Several days exposure to ambient temperatures will not
reduce activity. Stable at least 12 months when stored
properly.
Directions for use
1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water.
2. Add 10 µl 5x Reaction Buffer 4.5
3. Add 2.0 µl of Endo F2 to the reaction. Incubate 1 hour at 37°C.
Monitor cleavage by SDS-PAGE
The production host strain has been extensively tested and does not produce any detectable glycosidases.