Detection of Human, Mouse, and Rat Thioredoxin Reductase 1/TRXR1 by Western Blot.
Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line, NIH‑3T3 mouse embryonic fibroblast cell line, and C6 rat glioma cell line. PVDF membrane was probed with 0.1 µg/mL of Mouse Anti-Human Thioredoxin Reductase 1/TRXR1 Monoclonal Antibody (Catalog # MAB7428) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for Thioredoxin Reductase 1/TRXR1 at approximately 65 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Thioredoxin Reductase 1/TRXR1 in HeLa Human Cell Line by Flow Cytometry.
HeLa human cervical epithelial carcinoma cell line was stained with Mouse Anti-Human/Mouse/Rat Thioredoxin Reductase 1/TRXR1 Monoclonal Antibody (Catalog # MAB7428, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram), followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B). To facilitate intracellular staining, cells were fixed with paraformaldehyde and permeabilized with saponin.
Preparation and Storage
Sterile PBS to a final concentration of 0.5 mg/mL.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Thioredoxin Reductase 1/TRXR1
Thioredoxin reductase 1 (TRXR1) is an approximately 70 kDa member of the class-I pyridine nucleotide-disulfide oxidoreductase family. Human TRXR1 is 649 amino acids (aa) in length. Residues 151-152 constitute a propeptide that is deleted from the mature protein. Splicing variants produce five additional isoforms for human TRXR1. Isoform 2 has a 32 aa substitution for aa 107-138 and a deletion of aa 1-106. Isoform 3 has a deletion of aa 1-51 and a 49 aa substitution for aa 52-100. Isoform 4 is missing aa 1-98 and has a 3 aa substitution for aa 99-101. Isoform 5 has a deletion of aa 1-150. Residues 56-156 make up a glutaredoxin domain, and residues 520-632 constitute a pyridine nucleotide-disulphide oxidoreductase dimerization domain. In addition, there are three phosphotyrosines at positions 161, 163, and 281, and a selenocysteine at position 648. Human TRXR1 shares 74% and 70% aa sequence identity with mouse and rat TRXR1, respectively. Isoform 1 is involved in glutaredoxin activity as well as thioredoxin reductase activity, and it induces actin and tubulin polymerization, which leads to formation of cell membrane protrusions. Isoform 4 has been shown to enhance the transcriptional activity of the beta receptor only. Finally, isoform 5 mediates cell death induced by a combination of interferon-beta and retinoic acid. Isoform 1 is expressed mostly in the Leydig cells, but also in the ovary, spleen, heart, liver, kidney, and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in the kidney, uterus, testis, ovary, prostate, placenta, and fetal liver.
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