Human IgG4 | AbD18705_hIgG4_Pro
Recombinant Human IgG4 Kappa (Mutant) was analyzed under non-reducing, denaturing conditions (Lane 2) and reducing, denaturing conditions (Lane 3). Bands were visualized using Coomassie staining and the heavy (HC) and light chains (LC) are indicated. The molecular weight (kDa) of the marker proteins (Lane 1) are displayed on the left hand side of the image
UV280 chromatogram of a size exclusion chromatography run of recombinant Human IgG4 Kappa (Mutant). The larger peak corresponds to monomeric, fully assembled AbD18705_hIgG4_Pro. The smaller shoulder most likely contains dimers and aggregates
Recombinant Human IgG4 kappa (mutant), clone AbD18705_hIgG4_Pro is a recombinant human IgG4 antibody with a kappa light chain and a mutation in the core hinge region.
Clone AbD18705_hIgG4_Pro is specific for green fluorescent protein (GFP) and has no known reactivity with mammalian proteins or other antigens. This product is recommended for use as a standard in assays designed to measure IgG4 levels, or as a control antibody when using other human antibodies of the same isotype and subclass.
In addition to the tetrameric IgG structure, composed of two copies each of the heavy and light chains, wild type human IgG4 forms so-called half-molecules. This species contains only one heavy and one light chain. Half-molecules can assemble with an unrelated half-molecule to form bispecific tetrameric antibody species (Aalberse et al. 2002). Half-molecules of human IgG4 preparations can be detected as an additional species under denaturing, non-reducing conditions using SDS-PAGE, size exclusion chromatography or capillary electrophoresis. Mutation in the core hinge region of IgG4 prevents the formation of half-molecules (Bloom et al. 1997). Recombinant Human IgG4 kappa (mutant) does not display this additional species; half-molecules cannot be detected in SDS-PAGE or by size exclusion chromatography.
In addition to the mutant recombinant, Bio-Rad also offers recombinant Human IgG4 kappa in its wild type form (HCA195). Recombinant Human IgG4 lambda is also available in both wild type (HCA050) and mutant form (HCA246).
Clone AbD18705_hIgG4_Pro is specific for green fluorescent protein (GFP) and has no known reactivity with mammalian proteins or other antigens. This product is recommended for use as a standard in assays designed to measure IgG4 levels, or as a control antibody when using other human antibodies of the same isotype and subclass.
In addition to the tetrameric IgG structure, composed of two copies each of the heavy and light chains, wild type human IgG4 forms so-called half-molecules. This species contains only one heavy and one light chain. Half-molecules can assemble with an unrelated half-molecule to form bispecific tetrameric antibody species (Aalberse et al. 2002). Half-molecules of human IgG4 preparations can be detected as an additional species under denaturing, non-reducing conditions using SDS-PAGE, size exclusion chromatography or capillary electrophoresis. Mutation in the core hinge region of IgG4 prevents the formation of half-molecules (Bloom et al. 1997). Recombinant Human IgG4 kappa (mutant) does not display this additional species; half-molecules cannot be detected in SDS-PAGE or by size exclusion chromatography.
In addition to the mutant recombinant, Bio-Rad also offers recombinant Human IgG4 kappa in its wild type form (HCA195). Recombinant Human IgG4 lambda is also available in both wild type (HCA050) and mutant form (HCA246).
Product Details
- Product Form
- Human IgG4 antibody selected from the HuCAL® phage display library and expressed in a human cell line - liquid.
- Preparation
- Purified IgG prepared by affinity chromatography on Protein A
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.01% Thiomersal
- Immunogen
- Green fluorescent protein.
- Approx. Protein Concentrations
- Antibody concentration 0.5 mg/ml
Storage Information
- Storage
- Store at +4oC or at -20oC if preferred.
Storage in frost-free freezers is not recommended.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. - Guarantee
- 12 months from date of despatch
More Information
- UniProt
- P01834
- P01861
- Entrez Gene
- IGKC
- IGHG4
- GO Terms
- GO:0005515 protein binding
- GO:0003823 antigen binding
- GO:0005576 extracellular region
- GO:0006958 complement activation, classical pathway
- GO:0045087 innate immune response
- GO:0005624 membrane fraction
- GO:0006955 immune response
- Acknowledgements
- Sold under license of U.S. Patents 6753136, 7785859 and 8273688 and corresponding patents. This antibody was developed by Bio-Rad, Zeppelinstr. 4, 82178 Puchheim, Germany.
- Licensed Use
- For in vitro research purposes only, unless otherwise specified in writing by Bio-Rad.
- Regulatory
- For research purposes only
Applications of Human IgG4
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| ELISA |
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
- Technical Advice
- Recommended protocols and further information about HuCAL recombinant antibody technology can be found in the HuCAL Antibodies Technical Manual
Copyright © 2020 Bio-Rad Antibodies (formerly AbD Serotec)
Useful Reagents Available
| Description | Product Code | Applications | Pack Size | List Price | Quantity |
|---|---|---|---|---|---|
| Recombinant Human IgG4 Lambda | HCA050 | E | 0.1 mg |
|
|
| Recombinant Human IgG4 Kappa | HCA195 | E | 0.1 mg |
|
|
| Recombinant Human IgG4 Lambda (Mutant) | HCA246 | E | 0.1 mg |
|
Product Specific References
Further Reading
-
Labrijn, A.F. et al. (2009) Therapeutic IgG4 antibodies engage in Fab-arm exchange with endogenous human IgG4 in vivo.
Nat Biotechnol. 27 (8): 767-71. -
Wilkinson, I.C. et al. (2013) Monovalent IgG4 molecules: immunoglobulin Fc mutations that result in a monomeric structure.
MAbs. 5 (3): 406-17. -
Aalberse, R.C. & Schuurman, J. (2002) IgG4 breaking the rules.
Immunology. 105 (1): 9-19. -
Bloom, J.W. et al. (1997) Intrachain disulfide bond in the core hinge region of human IgG4
Protein Sci. 6:407-415
