Monoclonal Anti-HIV protease antibody produced in mouse

NA.41

Human immunodeficiency virus (HIV) protease expressed in the 5′ end of pol gene is part of gag-pol polyprotein. HIV protease has 99 amino acids. The monomers of the protein are inactive; homodimers of the protein are enzymatically active. The antibody 1696 recognizes free N-terminus of mature HIV protease (HIV-1 and HIV-2), an enzyme that hydrolyzes polyproteins of HIV viruses into functional proteins. The antibody 1696 does not react with the precursor.

Bacterially expressed full-length HIV-1 protease

HIV protease is an aspartyl protease which is essential for cleavage of viral progenitor polyprotein. Protease activity is critically essential for the life cycle of the virus. HIV protease cleaves gag protein into three larger fragments p24, p17 and p7, which are the core structural protein and essential for RNA packaging. Protease also cleaves gag-pol fusion protein of the virion. The favourable cleavage site of HIV protease is N-terminal to proline, like phenylalanine-proline, tyrosine-proline, which is uncommon for mammalian proteases. The cleavage happens after the budding of the virion from the infected cell surface, transform into a mature infectious virus. Lack of protease results in immature and non-infectious viral particles. Inhibitors targeted to HIV protease is the recent advancement in the treatment of HIV infection.

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Solution in phosphate buffered saline, pH 7.4, with 15 mM sodium azide.

mouse

unconjugated

purified immunoglobulin

primary antibodies

1696, monoclonal

buffered aqueous solution

human immunodeficiency virus

1 mg/mL

FUNC: suitable
immunoblotting: suitable
indirect ELISA: suitable

IgG1

wet ice

2-8℃

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