Human IgG4 Fc Protein
Catalog No: IGG4FC-HP001
- Species
- Human
- Expression System
- HEK293
- Tag
- Fc
- Activity
- Activity verified
Product overview
Recombinant Human IgG4 Fc Protein is expressed in HEK293 cells without tag. It contains amino acid residues Glu99-Gly326 (UniProt accession: P01861).
Product Details
- Molecular Aliases
- IGHG4
- Protein Length
- Glu99-Gly326
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 25.8 kDa. Due to glycosylation, the protein migrates to 30-35 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 90% as determined by HPLC
- Endotoxin
- Less than 0.1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display
Human IgG4 Fc on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Human IgG4 Fc is greater than 90% as determined by SEC-HPLC.
Loaded Human FcRn, His Tag (Cat. FRN-HM101) on Anti-His-Biosensor can bind Human IgG4 Fc, No Tag with an affinity constant of 30.30 nM as determined in BLI assay. (QC Test)
Human FcRn, His Tag (Cat. FRN-HM101) captured on CM5 Chip via Anti-His Antibody can bind Human IgG4 Fc, No Tag with an affinity constant of 0.10 μM as determined in SPR assay (Biacore T200).
Background
It is known as a IgG4-related disease and its differentiation is based on the analysis of IgG4 levels in the affected tissues. The IgG4-related disease is considered to be a generalized pathological process involving a wide spectrum of various disorders that may affect distant organs.
References
- Touzani F, Pozdzik A. New insights into immune cells cross-talk during IgG4-related disease. Clin Immunol. 2019;198:1-10. doi:10.1016/j.clim.2018.11.004
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