Immunoglobulin G Fc Fragment (IgG FC)

Immunoglobulin G Fc Fragment (IgG FC)
SKU
ATH16-16-090707-FC-1
Packaging Unit
1 mg
Manufacturer
Athens Research & Technology

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Protein Catagory: Immuneglobulins

Typ: Human

Molecular Weight: 50,000 Da

Immunogen: No

Compound Purity: ≥95% by SDS-PAGE., No reaction by IEP to antisera to human IgG-fab.

Applications: Flow Cytometry, ELISA, Antisera Production, In Vitro Diagnostics, Proteomics

References: - Zeng, J., et al., (2019), 'Rare missense variants in the human cytosolic antibody receptor preserve antiviral function', eLife, 8: pp. e48339. Available at: DOI: https://doi.org/10.7554/eLife.48339 - Zhang, P., et al., (2020), 'Mechanism- and Immune Landscape-Based Ranking of Therapeutic Responsiveness of 22 Major Human Cancers to Next Generation Anti-CTLA-4 Antibodies', Cancers, 12: pp. 284. Available at: doi:10.3390/cancers12020284 - Wang, X., et al., (2022), 'CD24-Siglec axis is an innate immune checkpoint against metaflammation and metabolic disorder', Cell Metabolism, 34: pp. 1088–1103. Available at: https://doi.org/10.1016/j.cmet.2022.07.005 - Liu M., et al., (2023), Soluble CTLA-4 mutants ameliorate immune-related adverse events but preserve efficacy of CTLA-4– and PD-1–targeted immunotherapy', Sci. Transl. Med., 15 (685), eabm5663. Available at: DOI: 10.1126/scitranslmed.abm5663 - Li, Y., et al., (2024), 'CD177 is a novel IgG Fc receptor and CD177 genetic variants affect IgG-mediated function', Front. Immunol. 15:1418539. Available at: doi: 10.3389/fimmu.2024.1418539

Product Description: The Fc (fragment crystallizable) region of immunoglobulin G, while not binding antigen, contains crucial biological activities and antigenic determinants. This homodimeric glycoprotein comprises CH2 and CH3 domains and mediates immune effector functions through interactions with Fc receptors, C1q, and FcRn. Fc fragments orchestrate antibody-dependent cellular cytotoxicity, complement-dependent cytotoxicity, and phagocytosis while controlling IgG's serum half-life via pH-dependent FcRn binding. The conserved N-linked glycosylation at Asn-297 is essential for structural stability and receptor interactions. Altered Fc glycosylation patterns correlate with autoimmune conditions including rheumatoid arthritis, where reduced galactosylation and sialylation indicate inflammatory disease states. Fc receptor polymorphisms are also associated with autoimmune disease development.
More Information
SKU ATH16-16-090707-FC-1
Manufacturer Athens Research & Technology
Manufacturer SKU 16-16-090707-FC-1
Package Unit 1 mg
Quantity Unit STK
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