Human Thioredoxin-1 Biotinylated Antibody

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Product Details
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Human Thioredoxin-1 Biotinylated Antibody Summary

Species Reactivity
Detects human Thioredoxin-1 in Western blots. In Western blots, approximately 25% cross-reactivity with recombinant human Thioredoxin-1 (aa 1‑81) is observed.
Polyclonal Goat IgG
Antigen Affinity-purified
E. coli-derived recombinant human Thioredoxin‑1
Accession # P10599
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.


Recommended Concentration
Western Blot
0.1 µg/mL
Recombinant Human Thioredoxin‑1 (Catalog # 1970-TX)

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
Reconstitution Buffer 1 (PBS)
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Size / Price
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.
  • 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-1

Thioredoxins (Trxs) are a group of small ubiquitous proteins in all living cells that are key regulators of cellular redox balance (1, 2). The mammalian Trx family has three members. The Trx-1, which is a secreted and cellular protein, the mitochondria-specific Trx-2, and the Trx-like cytosolic protein p32TrxL (3-5). The active site of mammalian Trxs contains two cysteines in the conserved sequence -Y-C-G-P-C-K-. In Trx-1 the conserved cysteine residues are in positions 32 and 35, respectively. Trxs exist either in a reduced or in an oxidized state when the two cysteines at the active site form an intramolecular disulfide bridge. NADPH and the flavoprotein thioredoxin reductase can convert the oxidized Trx into the reduced Trx. Trx-1 is the only extracellular occurring thioredoxin, and is secreted by lymphocytes, hepatocytes, fibroblasts, and several tumor cells. Plasma concentrations of Trx-1 are up to 6 nM (6). In cells, Trx-1 is localized predominantly in the cytoplasm. Small amounts have been detected in the nucleus and in association with the outside surface of the cells. Expression of Trx-1 is increased under various stress conditions such as hypoxia, elevated hydrogen peroxide concentrations, photochemical oxidative stress, and viral and bacterial infections. Biological functions of Trx-1 include growth factor activity, antioxidant properties, a cofactor that provides reducing equivalents, and transcriptional regulation (1, 2). The synovial tissue of rheumatoid arthritis patients produces increased levels of Trx-1 under oxidative stress conditions, and a correlation exists between the plasma levels of Trx-1 and the severity of the disease, making Trx-1 a biomarker for this pathological condition (7, 8).

  1. Holmgren, A. (1985) Annu. Rev. Biochem. 54:237.
  2. Powis, G. and W.R. Monfort (2001) Annu. Rev. Pharm. Toxicol. 41:269.
  3. Deiss, L.P. and A. Kimchi (1991) Science 252:117.
  4. Spyrou, G. et al. (1997) J. Biol. Chem. 272:2936.
  5. Miranda-Vizuete, A. et al. (1998) Biochem. Biophys. Res. Commun. 243:284.
  6. Nakamura, H. et al. (1997) Annu. Rev. Immunol. 15:147.
  7. Mourice, M.M. et al. (1999) Arthritis Rheum. 42:2430.
  8. Jikimoto, T. et al. (2001) Mol. Immunol. 38:765.
Entrez Gene IDs
7295 (Human)
Alternate Names
Thioredoxin1; Thioredoxin-1; TRDX;TRX;TRX1;Trx80;TXN; Trx1; TXN; TXN1

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