Monoclonal Anti-HIV protease antibody produced in mouse

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.

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

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

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.