Mouse IgG2a Fc, Tag Free (IGA-M5207) is expressed from human 293 cells (HEK293). It contains AA Glu 98 - Lys 330 (Accession # CAC20702).
Predicted N-terminus: Glu 98
This protein carries no "tag".
The protein has a calculated MW of 26.4 kDa. As a result of glycosylation, the protein migrates as 30-35 kDa under reducing (R) condition, and 55-60 kDa under non-reducing (NR) condition (SDS-PAGE).
Less than 1.0 EU per μg by the LAL method.
>90% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 100 mM Glycine, 150 mM 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.
Mouse IgG2a Fc, Tag Free on SDS-PAGE under reducing (R) and non-reducing (NR) conditions. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
Loaded Mouse FCGRT&B2M Heterodimer Protein, His Tag&Twin-Strep Tag (BLI verified) (Cat. No. FCM-M52W2) on NTA Biosensor, can bind Mouse IgG2a Fc, Tag Free(Cat. No. IGA-M5207) with an affinity constant of 7.73 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).
Loaded Mouse FCGRT&B2M Heterodimer Protein, His Tag (BLI verified) (Cat. No. FCM-M52W8) on NTA Biosensor, can bind Mouse IgG2a Fc, Tag Free(Cat. No. IGA-M5207) with an affinity constant of 5.75 nM as determined in BLI assay (ForteBio Octet Red96e) (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.