R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
TAP1 (E4T4F) Rabbit mAb #49671
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 68 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
TAP1 (E4T4F) Rabbit mAb recognizes endogenous levels of total TAP1 protein. This antibody does not cross-react with TAP2 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human TAP1 protein.
Background
CD8+ cytotoxic T cells recognize peptides presented by MHC class I molecules on the surface of infected cells and tumor cells. The transporters associated with antigen processing 1 and 2 (TAP1 and TAP2) form the TAP complex which resides on the ER membrane and transports peptides from the cytoplasm into the ER for loading onto MHC class I molecules (1-8). In addition, TAP localized to endosomal membranes is important for cross-presentation by dendritic cells (9,10). IFN-γ produced by T cells and NK cells in response to infection causes upregulation of TAP1 and TAP2, resulting in increased antigen presentation to T cells (11). Some viral proteins inhibit TAP function or downregulate TAP expression resulting in viral immune evasion (12,13). In addition, investigators have observed reduced TAP expression in a variety of tumor types, and it is thought to be one mechanism for tumor immune evasion (14).
- Trowsdale, J. et al. (1990) Nature 348, 741-4.
- Spies, T. et al. (1990) Nature 348, 744-7.
- Deverson, E.V. et al. (1990) Nature 348, 738-41.
- Monaco, J.J. et al. (1990) Science 250, 1723-6.
- Spies, T. and DeMars, R. (1991) Nature 351, 323-4.
- Kleijmeer, M.J. et al. (1992) Nature 357, 342-4.
- Kelly, A. et al. (1992) Nature 355, 641-4.
- Spies, T. et al. (1992) Nature 355, 644-6.
- Huang, A.Y. et al. (1996) Immunity 4, 349-55.
- Guermonprez, P. et al. (2003) Nature 425, 397-402.
- Bahram, S. et al. (1991) Proc Natl Acad Sci U S A 88, 10094-8.
- Früh, K. et al. (1995) Nature 375, 415-8.
- Bennett, E.M. et al. (1999) J Immunol 162, 5049-52.
- Steer, H.J. et al. (2010) Oncogene 29, 6301-13.
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