Recombinant Human TAPBPR Fc Chimera Protein, CF Summary
Accession # Q9BX59.2
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Measured by its ability to inhibit anti-CD3 antibody induced IL-2 secretion by human T cells. The ED50 for this effect 0.500‑10.0 μg/mL.
2 μg/lane of Recombinant Human TAPBPR Fc Chimera Protein (Catalog # 11171-TP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 75-90 kDa and 150-180 kDa, respectively.
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 human TAPBPR consists of a lumenal domain containing an IgV and IgC domain, a transmembrane domain, and a cytoplasmic tail which lacks an ER retention motif. Within the lumenal domain, mature human TAPBPR shares 70% and 71% amino acid sequence identity with mouse 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).
- Hermann, C. et al. (2015) Tissue antigens 85(3):155.
- Teng, M. et al. (2002) European Journal of Immunology 32:1059.
- Lin, Y. et al. (2021). EMBO Mol Med. 13(5):13404.
- Porter, K.M. et al. (2014) Immunology 142:289.
- Margulies, D. et al. (2020) Current Opinion in Immunology 64:71.
- Boyle, L.H. et al. (2013) PNAS 110:3465.
- Hermann, C. et al. (2013) Journal of Immunology 191(11):5743.
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