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IgG2b Fc

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Cat. No. Species Product Description Structure Purity Feature
IGB-M5203 Mouse Mouse IgG2b Fc Protein, Tag Free (MALS verified)
IGB-M5203-structure
IGB-M5203-sds
IGB-L5204 Llama Llama IgG2b Fc Protein, Tag Free (MALS verified)
IGB-L5204-structure
IGB-L5204-sds

Part of Bioactivity data

IGB-M5203-MALS-HPLC
Mouse IgG2b Fc, Tag Free (Cat. No. ) MALS images

The purity of Mouse IgG2b Fc, Tag Free (Cat. No. IGB-M5203) was 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.
  • Clinical and Translational Updates
      
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

    IGB-L5204-MALS-HPLC
    Llama IgG2b Fc, Tag Free (Cat. No. ) MALS images

    The purity of Llama IgG2b Fc, Tag Free (Cat. No. IGB-L5204) was more than 95% and the molecular weight of this protein is around 53-65 kDa verified by SEC-MALS.

Synonym Name

IgG2B,IgG2b Fc

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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