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Human Immunoglobulin G (IgG)
Native whole molecule polyclonal protein, purified from mulitple donor pool
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Proteins Synonyms: IgG, Immunoglobulin Gamma Source: Human Plasma Purity: ≥ 95% by SDS-PAGE Physical State: Lyophilized 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, Immunoglobulin Gamma
Description of Human Immunoglobulin G (IgG)
Human Immunoglobulin G (IgG) is a 150 kDa protein. Immunoglobulin G (IgG), the most abundant plasma antibody (8–18 mg/mL), comprises four subclasses (IgG1–4) with distinct effector functions mediated by structural variations in their Fc regions. IgG neutralizes pathogens through Fab-mediated antigen binding and Fc-dependent mechanisms, including complement activation (via C1q binding to IgG1/IgG3) and antibody-dependent cellular cytotoxicity (ADCC) through FcγRIIIa engagement on natural killer cells. IgG’s extended half-life (21 days) arises from pH-dependent FcRn recycling, which also facilitates placental transfer, conferring neonatal immunity. Clinically, IgG deficiencies manifest as recurrent sinopulmonary infections: selective IgG subclass deficiencies (e.g., IgG2 impairing antipolysaccharide responses), while agammaglobulinemia features near-absent IgG (<200 mg/dL). Autoimmune disorders exhibit subclass-specific involvement-IgG4 drives MuSK myasthenia gravis through functional blockade, whereas IgG1/IgG3 mediate tissue damage in pemphigus via complement activation. Therapeutically, intravenous IgG (IVIG) at 2 g/kg modulates immunity in Guillain-Barré syndrome by Fc receptor saturation and anti-idiotypic effects. Diagnostic applications leverage IgG’s specificity in serological assays, with subclass profiling guiding immunodeficiency management.
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 (IgG) at -20°C.
Applications
ELISA, In Vitro Diagnostic, Proteomics, Biotherapeutics.
Citations/Publications
Chan, A. S. H., et al., (2016) 'Imprime PGG-Mediated Anti-Cancer Immune Activation Requires Immune Complex Formation', PLoS ONE, 11(11): e0165909. Available at: doi:10.1371/journal.pone.0165909
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
Kammeijer, G. S. M., et al., (2016), 'Dopant Enriched Nitrogen Gas Combined with Sheathless Capillary Electrophoresis−Electrospray Ionization-Mass Spectrometry for Improved Sensitivity and Repeatability in Glycopeptide Analysis', Anal. Chem., 88: pp. 5849−5856. Available at: DOI: 10.1021/acs.analchem.6b00479
Kurupati, R., et al., (2016), 'The Role of Neutrophil Proteins on the Amyloid Beta-RAGE Axis', Oncotarget., 7(39): pp. 62898-62911. Available at:doi: 10.18632/oncotarget.11704.
Bai, Y., et al., (2017), 'Rapid fluorescence detection of immunoglobulin E using an aptamer switch based on a bindinginduced pyrene excimer', Anal. Methods, 9: pp. 3962-3967. Available at: DOI: 10.1039/c7ay01308f
Shipped with ice packs
Gel Scan of Human Immunoglobulin G (IgG)
| 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
