The monomeric structure of immunoglobulin G (IgG) consists of two identical heavy chains and two identical light chains with molecular weight of 50kDa and 25kDa, respectively. The primary structure of this antibody also contains disulfide bonds involved in linking the two heavy chains, linking the heavy and light chains and resides inside the chains. IgG is further subdivided into four classes namely, IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity (Fab fragments).
Anti-Rabbit IgG (whole molecule), F(ab′)2 fragment–Cy3 antibody produced in sheep binds to all rabbit Igs and is useful when trying to avoid background staining due to the presence of Fc receptors.
Anti-Rabbit IgG (whole molecule), F(ab′)2 fragment-Cy3 antibody produced in sheep may be used for immunohistochemistry at a dilution of 1:100 and for immunocytochemistry.
1 mL in glass bottle
IgG antibody subtype is the most abundant of serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids and provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defense of the neonate against infections. The coupling of Cy3 to Anti-Rabbit IgG (whole molecule), F(ab′)2 fragment antibody allows for the visualization of proteins by fluorescent microscopy.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide
Cy is distributed under license from Amersham Biosciences Limited.
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