A portion of amino acids 765-794 from the human protein was used as the immunogen for this TAP1 antibody.
TAP (Transporter associated with antigen processing) is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding. TAP is also inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP is down-regulated by human Epstein-barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules. TAP1 and TAP2 form a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP, inducible by interferon gamma, belongs to the ABC transporter family, MDR subfamily.
