Monoclonal Anti-β-COP antibody produced in mouse

Monoclonal Anti- β-COP (mouse IgG1 isotype) is derived from the M3A5 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. COPs (coatomer proteins) have a molar mass of 110 kDa and its primary structure is homologous to the β-adaptin component of clathrin-coated vesicles.

The coatomer (approx. 550kDa) consists of proteins designated α-, β-, γ-, and δ-COP, together with substoichiometric amounts of several other proteins.

microtubule-associated protein from goose brain.

Monoclonal Anti-β-COP antibody produced in mouse has been used:

• for the localization of β-COP using immunoprecipitation
• in immunocytochemistry
• in immunoblotting
• with other antibodies to Golgi proteins to study the role and relationships of this protein in the cell

COPs (coatomer proteins) are transiently attached to the vesicles involved in transport within the Golgi complex and possibly between the rough ER and Golgi complex.

The antibody recognizes an epitope shared by β-COP (110 kDa) found in most tissue culture lines, and by a doublet of brain microtubule-associated protein (MAP2, 270-300 kDa). The antibody stains a reticular structure in the perinuclear area of non-neuronal cells (the periphery of Golgi complex and a population of coatomers scattered throughout the cytoplasm) in tissues from different species and cell processes, as well as cell bodies in chicken brain neuronal cells. It has been used for studies on the effects of various agents that influence energy status, disrupt the Golgi complex, or alter the activity of G-proteins or small GTP-binding proteins on the cellular localization of β-COP. The antibody may be used for the immunoaffinity purification of the protein.

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