Anti-Horse IgG (Fc specific)-Peroxidase antibody produced in goat

The immunoglobulin IgG from horse comprises six subtypes. The subtypes share high sequence homology. Immunoglobulin super-family have a common structure, comprising two heavy (H) chains and two light (L) chains, held together by disulfide linkages. The heavy chain has one variable N-terminal region and three to four constant (CH1-CH4) C-terminal regions. The L chain comprises of one variable N-terminal region and a constant C-terminal region.

This product was prepared from monospecific antiserum by immunoaffinity chromatography using Horse IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Peroxidase, Anti-Goat Serum, Horse IgG, Horse IgG F(c) and Horse Serum. No reaction was observed against Horse IgG F(ab′)2.

Horse IgG F(c) fragment

Immunoglobulin IgG digestion by papain results in the generation of fragment antigen binding (Fab). Pepsin digestion of IgG generates fragment crystallisable (Fc). The Fc region of IgG antibody has enormous therapeutic potential and is exploited for the development of therapeutic antibodies. Normal serum IgG levels (400-800 mg/dl) along with total serum proteins and serum globulin is essential in foals to alleviate the risk of developing failure of transfer of passive immunity(FTPI).

Antibody format: IgG

Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

Reconstitute with 1.0 mL deionized water (or equivalent).

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