IdeS Protease (40U/μL)
IdeS Protease, or Immunoglobulin G-degrading enzyme of Streptococcus pyogenes, is a highly specific cysteine protease that cleaves IgG at a precise site within the antibody's hinge region, yielding intact F(ab’)2 and Fc fragments. This enzyme demonstrates exceptional substrate selectivity, recognizing human IgG and IgG from various animal species, including rabbit, monkey, sheep, and human-animal chimeric IgG. Recombinantly expressed in E. coli, IdeS Protease is produced with high purity and activity.
Specifications:
- Source : Recombinant E. coli expression
- Purity : ≥95%, verified by SDS-PAGE and HPLC
- Molecular Weight : 35.3 kDa
- Enzyme Concentration : 40 U/μL
- Storage Buffer : 50 mM sodium phosphate, 150 mM NaCl (pH 6.6), 50% glycerol
- Unit Definition : One unit of activity cleaves >95% of 1 μg recombinant monoclonal IgG in 30 minutes at 37°C
- Storage and Shipping : Store at -15°C to -25°C for up to one year.
Specifications:
- Source : Recombinant E. coli expression
- Purity : ≥95%, verified by SDS-PAGE and HPLC
- Molecular Weight : 35.3 kDa
- Enzyme Concentration : 40 U/μL
- Storage Buffer : 50 mM sodium phosphate, 150 mM NaCl (pH 6.6), 50% glycerol
- Unit Definition : One unit of activity cleaves >95% of 1 μg recombinant monoclonal IgG in 30 minutes at 37°C
- Storage and Shipping : Store at -15°C to -25°C for up to one year.
Figure 1.
A. HPLC analysis of MAG3-Cet-F(ab′)2 and MAG3-Cet-Fc after digestion of MAG3-Cet with IdeS protease.
B. HPLC analysis of the mixture from panel A after incubation with protein A beads. The protein A beads effectively removed the residual MAG3-Cet and most of the MAG3-Cet-Fc.
