Where can I find the protein concentration?

The protein concentration of each product is listed on the Certificate of Analysis. This value is determined for each individual lot and reflects the actual concentration (mg/mL) of the material you received.

Where can I find the recommended storage conditions?

Storage conditions are listed on both the product datasheet and the Certificate of Analysis. These recommendations are based on internal stability assessments and are intended to maintain protein integrity and activity.

What should I do if my product arrives warm, partially thawed, or damaged?

Please contact Athens Bioscience with your order number and lot number. Our technical support team will assist you promptly.

Where can I find the final buffer composition?

The final buffer formulation is provided on the Certificate of Analysis. This includes buffer components, pH, and whether the product was supplied as a liquid or lyophilized powder.

Immunoglobulin G, Fc Fragment, Immunogen Grade

Name: Immunoglobulin G, Fc Fragment, Immunogen Grade
SKU: 16-16-090707-FC-IMM-1MG
Availability: InStock

IgG FC IMM

While lacking antigen binding capacity, IgG Fc orchestrates antibody-dependent cytotoxicity, complement-dependent cytotoxicity, and phagocytosis. It mediates immune function through FC-receptor binding.

Purity: ≥99% (SDS-PAGE)

Source: Human Plasma

Molecular Weight: 50 kDa

Form: Frozen

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Product Description

Role of protein in biology

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.

Common research uses

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.

Common uses include therapeutics research, immune system research, flow cytometry assays, antisera production.