Anti-Rabbit IgG (whole molecule)–Alkaline Phosphatase antibody produced in goat

Anti-rabbit IgG (whole molecule) is produced in goat using purified rabbit IgG as the immunogen. Antibody is isolated from anti-rabbit IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins that do not specifically bind to rabbit IgG. The antibody preparation is solid phase adsorbed with human serum proteins to ensure minimal cross reactivity in tissue or cell preparations. Anti-Rabbit IgG is conjugated to alkaline phosphatase by protein cross linking with 0.2% glutaraldehyde.
Specificity of the antiserum is determined by immunoelectrophoresis prior to conjugation, versus normal rabbit serum and rabbit IgG. Identity and purity of the antibody is established by immunoelectrophoresis prior to conjugation. Electrophoresis of the product followed by diffusion versus anti-goat IgG and anti-goat whole serum results in single arcs of precipitation.

IgGs are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins.

Immunoglobulin G (IgG) belongs to the immunoglobulin family and is a widely expressed serum antibody. It consists of a gamma (γ) heavy chain in the constant (C) region. The monomeric 150kDa structure of IgG constitutes 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). The third fragment does not possess antigen-binding activity and is known as fragment crystallizable (Fc).

Purified rabbit IgG

Citrullination of antithrombin by PADI4 was analyzed by ELISA using alkaline phosphatase conjugated goat anti-rabbit IgG as the secondary diluted at 1:5000 in 0.05M carbonate/bicarbonate buffer (Ph 9.6).

Goat anti-rabbit IgG (whole molecule)-alkaline phosphatase antibody can be used for western blot and ELISA

It can also be used for immunohistochemistry (1:50) and dot bot (1:30,000) assays.

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl₂, 10 mM glycine, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide

Adsorbed to reduce background staining with human samples.

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