Biotinylated Mouse IgE Protein
Catalog No: IGE-MB001
- Species
- Mouse
- Expression System
- HEK293
- Tag
- with a His, Avi
- Activity
- Activity verified
Product overview
Recombinant Biotinylated Mouse IgE Protein is expressed in HEK293 cells with with a His tag and Avi tag at the C-terminus. It contains amino acid residues Asp198-Ser421 (UniProt accession: P06336).
Product Details
- Molecular Aliases
- Ig epsilon chain C region; IgE
- Protein Length
- Asp198-Ser421
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 28.2 kDa. Due to glycosylation, the protein migrates to 35-45 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22 μm 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
Biotinylated Mouse IgE on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Biotinylated Mouse IgE is greater than 95% as determined by SEC-HPLC.
Immobilized Human Fc epsilon RI alpha, hFc Tag at 1μg/ml (100μl/well) on the plate. Dose response curve for Biotinylated Mouse IgE, His Avi tag with the EC50 of 42.0ng/ml determined by ELISA. (QC Test)
Human Fc epsilon RI alpha, hFc Tag captured on CM5 Chip via Protein A can bind Biotinylated Mouse IgE, His-Avi tag with an affinity constant of 0.42 nM as determined in SPR assay (Biacore T200).
Background
Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, FcεRI and CD23 (FcεRII). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE-Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE-CD23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule.
References
- Sutton BJ, Davies AM. Structure and dynamics of IgE-receptor interactions: FcεRI and CD23/FcεRII. Immunol Rev. 2015 Nov;268(1):222-35. doi: 10.1111/imr.12340. PMID: 26497523.
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