MMTV Antibody

Background

This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Enzyme, and Viral research. Mouse mammary tumor virus capsid is a polyprotein that is cleaved by aspartyl protease during or after the release of the virion from the plasma membrane. After entering the cell, reverse transcriptase converts the viral dimeric RNA genome into dsDNA in the cytoplasm. Displaying DNA polymerase activity and RNase H activity, this enzyme copies either DNA or RNA templates and cleaves the RNA strand of the RNA-DNA heteroduplex in a partially processive 3' to 5' endonucleasic mode. tRNS binds to the primer at the 5' end of the viral RNA. Reverse transcriptase uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis proceeding through the U5 region and ending after the repeated region. This RNA-DNA heteroduplex is digested by the RNase H and hybridizes with the identical R region at the 3' end of the viral RNA. RNase H then digests the RNA template except for a polypurine tract situated at the 5' end of the genome. RNase H probably can proceed both in a polymerase-dependent and a polymerase-independent mode. Reverse transcriptase also performs DNA-directed plus-strand DNA synthesis using the polypurine tract that has not been removed by RNase H as primers. Polypurine tract and tRNA primers are then removed by RNase H and the 3' and 5' ssDNA primer binding site regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by reverse transcriptase to the primer binding site and polypurine tract ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats at both ends. Anti-MMTV Antibody is ideal for researchers interested in Cancer, Enzyme, and Viral research.