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Your Position: Accueil > Protein > IgG2b Fc > IGB-M5203

Mouse IgG2b Fc Protein, Tag Free (MALS verified)

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  • Synonym
    IgG2B,IgG2b Fc
  • Source
    Mouse IgG2b Fc, Tag Free(IGB-M5203) is expressed from human 293 cells (HEK293). It contains AA Glu 97 - Lys 335 (Accession # P01867-2).
    Predicted N-terminus: Glu 97
  • Molecular Characterization
    IgG2b Fc Structure

    This protein carries no "tag"

    The protein has a calculated MW of 26.7 kDa. The protein migrates as 33-35 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

    >90% as determined by SEC-MALS.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 100 mM Glycine, 25 mM Arginine, 150 mM NaCl, pH7.5 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • 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:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
IgG2b Fc SDS-PAGE

Mouse IgG2b Fc, Tag Free on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

SEC-MALS
IgG2b Fc MALS images

The purity of Mouse IgG2b Fc, Tag Free (Cat. No. IGB-M5203) is more than 90% and the molecular weight of this protein is around 56-66 kDa verified by SEC-MALS.

  • Background
    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. Ig gamma-2 chain Fc region contains two constant regions of IgG2 H chain (CH2, CH3).
  • Clinical and Translational Updates

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