Anti-Guinea Pig IgG (whole molecule)−Peroxidase antibody produced in goat

IgG consists of four sub-classes, like IgG1, IgG2, IgG3, and IgG4. IgG is composed of four polypeptide chains-two heavy chains (γ chains) and two light chains (κ or λ chains) which are linked by inter-chain disulfide bonds. The heavy chains consist of a N-terminal variable domain (VH) and three constant domains (CH1, CH2, CH3). A hinge region exists between the CH1 and CH2 region. The light chains have one N-terminal variable domain (VL) and one constant domain (CL).

Purified guinea pig IgG

Anti-H. pylori IgGs in guinea pig sera was measured by ELISA using HRP-conjugated goat anti-guinea pig IgG (A 7289) at a dilution of 1:2000 in 1% BSA/PBS for 1 hour at 37°C.

Anti-Guinea Pig IgG (whole molecule)-Peroxidase antibody is suitable for use in immunocytochemistry and ELISA.

Guinea pig IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-guinea pig IgGs conjugated to detectable substrates are useful tools for the analysis of target proteins. Anti-Guinea Pig IgG (whole molecule)-Peroxidase antibody is specific for guinea pig IgG.

IgGs are glycoprotein antibodies that modulate several immune responses. It plays a major role in providing immunity to the infant from the mother via the placenta. IgG activates the complement system and regulates the antibody-dependent cell-mediated cytotoxicity (ADCC).

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin with preservative.

Antiserum is developed in goat using purified guinea pig IgG as the immunogen. Antibody is isolated from goat anti-guinea pig IgG antiserum by immunospecific purification which removes essentially all goat serum proteins, including immunoglobulins that do not specifically bind to guinea pig IgG. Goat anti-guinea pig IgG is conjugated to Sigma Horseradish Peroxidase, Type VI (Product No. P 8375) by a modification of the periodate method of Wilson and Nakane.

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