R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
TRXR1 (D1T3D) Rabbit mAb #15140
Filter:
- WB
- IHC
Supporting Data
| REACTIVITY | H M R Hm Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 55 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Hm-Hamster
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunohistochemistry (Paraffin) | 1:100 |
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
TRXR1 (D1T3D) Rabbit mAb recognizes endogenous levels of total TRXR1 protein.
Species Reactivity:
Human, Mouse, Rat, Hamster, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly412 of human TRXR1 protein.
Background
TRXR1 (thioredoxin reductase 1) is a selenocysteine-containing protein that is involved in redox homeostasis (1-6). Its canonical target is thioredoxin, another redox protein (1). Together, they are involved in many functions such as antioxidant regulation (3-6), cell proliferation (2,3,5), DNA replication (2,3), and transcription (3,5). TRXR1 is also capable of reducing a wide array of cellular proteins (1,3). Selenium deficiency, either by diet modification (2,6) or introduction of methylmercury (4), hinders proper expression and function of TRXR1. It is possible that this effect, which results in a higher oxidative state, is a result of the selenocysteine codon (UGA) being read as a STOP codon in the absence of adequate selenium (4). The functions of TRXR1 in cell proliferation and antioxidant defense make it a potential therapeutic target.
- Turanov, A.A. et al. (2010) Biochem J 430, 285-93.
- Gasdaska, P.Y. et al. (1995) FEBS Lett 373, 5-9.
- Gromer, S. et al. (2004) Med Res Rev 24, 40-89.
- Usuki, F. et al. (2011) J Biol Chem 286, 6641-9.
- Pappas, A.C. et al. (2008) Comp Biochem Physiol B Biochem Mol Biol 151, 361-72.
- Müller, M. et al. (2010) Genes Nutr 5, 297-307.
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