Biotinylated 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 98
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.
Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
The biotin to protein ratio is 0.7-1 as determined by the HABA assay.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
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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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
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).
Immunoglobulin 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.