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, Immunology and Nuclear Signaling research. Feline immunodeficiency virus (FIV) belongs to the lentivirus family. This family is characterized by assembly of the viral capsid at either the plasma membrane or at the limiting membrane of late endosomes. The capsid assembles from the viral Gag polyprotein. Upon release of a budding virion, Gag precursor protein is cleaved by the viral protease into its mature products, namely Matrix Protein, Capsid and Nucleocapsid. Matrix Protein, located at the N-terminus of the Gag polyprotein, is usually myristylated during protein translation, prior to the later events of virus assembly. The myristate moiety is believed to be sequestered within the Matrix Protein during protein translation and later facilitates membrane binding upon exposure resulting from conformational changes. Essential functions attributed to the Matrix Protein of lentiviruses include targeting newly synthesized Gag precursor proteins to the site of virus assembly by binding with cellular components such as phosphatidylinositides. In the mature virus particle, the Matrix Protein provides internal structure to the virion within the capsid, but is not exposed at the surface of the particle. Based on studies with HIV, it is postulated that FIV Matrix Protein may also serve additional functions, including nuclear localization of the viral core upon entry of the virus into a new host cell.
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids from an internal region of FIV Matrix Protein p15.