Measured by its binding ability in a functional ELISA. Immobilized Human Fc-gamma RII-a(CD32a) at 1 μg/mL (100 μL/well) can bind IgG1 Fc with a linear range of 0.156-3.47 μg/mL.
Purity
> 95% by SDS-PAGE.
Endotoxin
<0.1EU/ug
Formulation
Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (5 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR ) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.
Store the lyophilized protein at -20°C to -80°C for long term. After reconstitution, the protein solution is stable at -20°C for 3 months, at 2-8°C for up to 1 week.
Reconstitution
Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water.