- SynonymIgG2A
- SourceBiotinylated Mouse IgG2a Fc, Avitag (IGA-M8210) is expressed from human 293 cells (HEK293). It contains AA Glu 98 - Lys 330 (Accession # P01863).Predicted N-terminus: Glu 98Request for sequence
- Molecular Characterization
This protein carries an Avi tag at the C-terminus.
The protein has a calculated MW of 28.2 kDa. The protein migrates as 36 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- BiotinylationBiotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
- Biotin:Protein RatioThe biotin to protein ratio is 0.7-1 as determined by the HABA assay.
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>95% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.
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- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Biotinylated Mouse IgG2a Fc, Avitag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Immobilized Recombinant Protein A at 5 μg/mL (100 μL/well) can bind Biotinylated Mouse IgG2a Fc, Avitag (Cat. No. IGA-M8210) with a linear range of 0.8-13 ng/mL (QC tested).
Immobilized Mouse CD16-2, His Tag (Cat. No. FC4-M52H3) at 5 μg/mL (100 μL/well) can bind Biotinylated Mouse IgG2a Fc, Avitag (Cat. No. IGA-M8210) with a linear range of 0.01-0.313 μg/mL (Routinely tested).
- BackgroundImmunoglobulin G2 (IgG2) is a member of many immunoglobulin G developed and secreted by effective B cells. In wake of cutting by pepsin, IgG is divided into two F(ab)s with one antigen binding site and a high conserved Fc segment. The Fc segment bears a highly conserved N-glycosylation site. There are two members of IgG2: IgG2a and IgG2b. It was found that IgG2a was superior to IgG1 in activating complement. The glycosylation of the circulating immunoglobulin-γ (IgG) antibody molecules changes in rheumatoid arthritis.
- References
- (1)Sikorav J.-L., et al., 1980, Nucleic Acids Res. 8:3143-3155.
- (2)Ollo R., et al., 1981, Proc. Natl. Acad. Sci. U.S.A. 78:2442-2446.
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