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Clathrin Structure Characterized With Monoclonal Antibodies. I. Analysis of Multiple Antigenic Sites

Clathrin Structure Characterized With Monoclonal Antibodies. I. Analysis of Multiple Antigenic Sites

F M Brodsky

J Cell Biol. 1985 Dec;101(6):2047-54.

PMID: 2415533

Abstract:

Three monoclonal antibodies that react with previously undefined antigenic determinants on the clathrin molecule have been produced and characterized. They were isolated from a fusion between myeloma cells and popliteal lymphocytes from SJL mice that had received footpad injections of human brain clathrin. This protocol was chosen to favor the production of antibodies to poorly immunogenic proteins and thereby increase the repertoire of anti-clathrin monoclonal antibodies. One antibody (X16) reacts preferentially with the heavier of the two clathrin light chains (LCa) when it is not associated with heavy chain. This specificity is different from that of the anti-LCa antibody, CVC.6, which has preferential reactivity with heavy chain-associated LCa. In addition, X16 and CVC.6 bound simultaneously to LCa, confirming that they react with different sites. The other two antibodies produced, X19 and X22, react with two different determinants on the clathrin heavy chain, based on immunoprecipitation, Western blot, and binding studies. Competitive binding studies with anti-clathrin monoclonal antibodies showed that they define a total of five distinct antigenic determinants on bovine clathrin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42413819	Monoclonal Anti-Clathrin Heavy Chain antibody produced in mouse			Price
IAR42413820	Anti-Clathrin Light Chain antibody, Mouse monoclonal			Price

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