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Human Immunoglobulin G Fab Fragment (IgG Fab)
IgG Fab Fragment generated from multiple donor native IgG Polyclonal, whole molecule
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Proteins Synonyms: IgG Fab Source: Human Plasma Purity: ≥ 95% by SDS-PAGE. No reaction by IEP to antisera to human IgG-fc. Physical State: Frozen in 20 mM phosphate, pH 7.4, with 150 mM NaCl and 0.05% NaN3. Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
IgG Fab
Description of Human Immunoglobulin G Fab Fragment (IgG Fab)
Human Immunoglobulin G Fab Fragment (IgG Fab) is a 50 kDa protein. The IgG Fab (Fragment antigen-binding) fragment is a monovalent proteolytic product of Immunoglobulin G. Each Fab fragment retains the variable domains (VH and VL) responsible for antigen specificity while lacking the Fc-mediated effector functions, enabling targeted antigen neutralization without immune activation. This structural configuration prevents cross-linking-induced precipitation or cellular "patching/capping, " making Fab fragments ideal for precise antigen targeting in solution or on cell surfaces. Diagnostically, Fab fragments enable multiplex immunoassays by preventing Fc-mediated cross-reactivity, facilitating simultaneous detection of multiple antigens in flow cytometry and immunohistochemistry. Their monovalent nature ensures minimal background noise in assays requiring high specificity. Emerging applications include autoimmune disease management, where Fab fragments neutralize autoantibodies while circumventing complement activation. By combining targeted binding with reduced immunogenicity, IgG Fab fragments represent a versatile tool in both clinical and research settings.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human Immunoglobulin G Fab Fragment (IgG Fab) at -20°C.
Applications
Biotherapeutics, Flow Cytometry, Immunohistochemistry, Antisera Production.
Citations/Publications
Padmanabhan, A., et al., (2017), 'IVIg for Treatment of Severe Refractory Heparin-Induced Thrombocytopenia', CHEST, 152(3): pp 478-485. Available at: http://dx.doi.org/10.1016/j.chest.2017.03.050
Fletcher, N. A., et al., (2016), 'Controlled delivery of antibodies from injectable hydrogels', Materials Science and Engineering C 59: pp 801–806. Available at: https://doi.org/10.1016/j.msec.2015.10.096
Karau, M. J., et al., (2017), 'Passive therapy with humanized antistaphylococcal enterotoxin B antibodies attenuates systemic inflammatory response and protects from lethal pneumonia caused by staphylococcal enterotoxin B-producing Staphylococcus aureus', VIRULENCE. 8(7): pp 1148–1159. Available at: https://doi.org/10.1080/21505594.2016.1267894
Kilgore, R., et al., (2023), 'Development of peptide affinity ligands for the purification of polyclonal and monoclonal Fabs from recombinant fluids', Journal of Chromatography A 1687: pp 463701. Available at: https://doi.org/10.1016/j.chroma.2022.463701
Ngatuni, M. J., et al., (2018), 'Novel Random Triblock Copolymers for Sustained Delivery of Macromolecules for the Treatment of Ocular Diseases', AAPS PharmSciTech, 19(8): pp 3871-3885. Availablae at: DOI: 10.1208/s12249-018-1172-3
Shipped with dry ice
Gel Scan of Human Immunoglobulin G Fab Fragment (IgG Fab)
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
Paying by bank transfer
