Recombinant Mouse TAPBPR Fc Chimera Protein, CF New

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Preparation and Storage

Background:

TAP-binding protein-like (TAPBPL), also known as TAP binding protein-related (TAPBPR) and Tapasin-related protein (TAPASINR) is a transmembrane protein of the Immunoglobulin (Ig) superfamily (1, 2). TAPBPR was originally isolated as a homologue to TAPASIN but more recently was identified as a novel B7 family-related molecule since it shares sequence, structural, and functional similarities to B7 family members (3). Mature mouse TAPBPR consists of a lumenal domain containing an IgV and IgC domain, a transmembrane domain, and a cytoplasmic tail.  Within the lumenal domain, mature mouse TAPBPR shares 70% and 87% amino acid sequence identity with human and rat TAPBPR, respectively. Multiple alternatively spliced TAPBPR isoforms are known to exist with unique properties (4).TAPBPR is widely expressed and, similar to TAPASIN, functions as a both a chaperone protein and peptide editor of MHC class I, but in a peptide‑loading complex (PLC) independent manner (5, 6). TAPBPR decreases the rate at which MHC class I molecules mature through the secretory pathway, a role which could be important for peptide selection by MHC class I molecules (7). TAPBPR is also expressed on the surface of T cells and antigen-presenting cells (APCs) and plays an inhibitory role in the proliferation and activation of T cells (4). TAPBPR can be expressed on various cancer cells like leukemia and has the potential to be used in the treatment of autoimmune diseases and transplant rejection, as well as cancer (4).