Recombinant Human Thioredoxin 80 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Thioredoxin 80 Protein, CF Summary

Details of Functionality
Measured by its ability to induce IFN-gamma secretion by human peripheral blood mononuclear cells (PBMC) in the presence of IL-2. Pekkari, K. et al. (2001) Blood 97:3184. The ED50 for this effect is 3-9 µg/mL in the presence of 8 ng/mL of rhIL-2.
Source
E. coli-derived human Thioredoxin-80 protein
Val2-Lys81
Accession #
N-terminal Sequence
Val2
Structure / Form
Noncovalently-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
TXN
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
9 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris, EDTA and DTT.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Thioredoxin 80 Protein, CF

  • Thioredoxin80
  • Thioredoxin-80

Background

Human thioredoxin 80 (Trx80) is a proteolytic cleavage product of a larger precursor termed thioredoxin. Thioredoxin (Trx) ia a 12 - 14 kDa nonglycosylated monomeric 105 amino acid (aa) polypeptide that is synthesized by a wide variety of cells (1 - 3). Trx is a member of the thioredoxin family of proteins that contains a key Cys-X-Tyr-Cys motif that participates in redox reactions (4). Trx is considered the principal disulfide reductase in cells (2, 5). Although it possesses no definitive signal sequence, Trx is secreted and is considered to be the only extracellularly occurring thioredoxin. Trx80, by contrast, is a 10 kDa proteolytic cleavage product of Trx that contains the N-terminal 80 aa residues of Trx (5, 6). This form contains the key CGYC motif found in Trx and shares the same 3-dimensional globular structure as Trx. However, the differences between the molecules are significant. Trx80 lacks Trx’s C-terminus and has no oxidoreductase activity. Trx also circulates as a monomer while Trx80 exists a nondisulfide-linked dimer. Endogenous Trx80 is localized on the plasma membrane of monocytes and macrophages, while Trx is found on the cell surface of various cell types (7). Trx80 also shows significant cytokine activity while Trx has none (5). Cytokine activities attributed to Trx80 include the enhancement of eosinophil ADCC (2), the inducement of monocyte proliferation and maturation to a unique IL-10 secreting phenotype, and the upregulation of monocyte membrane CD14, CD40, CD54/ICAM-1, and CD86/B7 (5, 8). A receptor for Trx80 has not been identified. Human Trx80 is 89% aa identical to mouse and rat Trx80, and 35% aa identical to B. subtilis Trx.

  1. Wollman, E.E. et al. (1988) J. Biol. Chem. 263:15506.
  2. Balcewicz-Sablinska, M.K. et al. (1991) J. Immunol. 147:2170.
  3. Yamawaki, H. et al. (2003) Circ. Res. 93:1029.
  4. Rundlof, A.-K. and E. Arner (2004) Antioxid. Redox Signal. 6:41.
  5. Pekkari, K. and A. Holmgren (2004) Antioxid. Redox Signal. 6:53.
  6. Nakamura, H. (2004) Antioxid. Redox Signal. 6:15.
  7. Pekkari, K. et al. (2000) J. Biol. Chem. 275:37474.
  8. Pekkari, K. et al. (2004) Blood 105:1598.

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Bioinformatics

Gene Symbol TXN
Entrez
Uniprot