Thioredoxin Active Protein | Txn1 active protein

Thioredoxin, Recombinant, Human

Cat. Num. AAA635789

• Gene Names: Txn1; ADF; Txn; Trx1; AW550880
• Purity: Highly Purified; 90% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified. Endotoxin: < 0.1ng/ug (1EU/ug)
• Synonyms: Thioredoxin; Recombinant; Human; Txn1 active protein

• Host: Recombinant, human (E Coli)
• Purity/Purification: Highly Purified; 90% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified. Endotoxin: < 0.1ng/ug (1EU/ug)
• Form/Format: Supplied as a lyophilized powder in 20mM PBS, pH 7.4. Reconstitute in sterile ddH2O. Can be further diluted to other aqueous solutions.

• Biological Activity: The specific activity was found to be ~3IU/mg. Activity was assayed by measuring the change in absorbance at 650nm at 25 degree C using 0.13uM bovine insulin containing 0.33mM DTT (pH 6.5).
• Preparation and Storage: Lyophilized powder may be stored at -20 degree C. Reconstitute with sterile ddH2O. Aliquot and store at -20 degree C. Reconstituted product is stable for 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for Txn1 active protein

Thioredoxins are small disulphide -containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in refolding proteins expressed in E. coli. To this end, thioredoxin has been shown to act as a protein disulfide isomerase.

Recombinant human Thioredoxin is a single, non-glycosylated, polypeptide chain of 96aa having a molecular mass of 11.9kD. The pI is 4.67.

Product Categories/Family for Txn1 active protein

Molecular Biology; MB-Thioredoxin

NCBI and Uniprot Product Information

• NCBI GI #: 6755911
• NCBI GeneID: 22166
• NCBI Accession #: NP_035790.1
• NCBI GenBank Nucleotide #: NM_011660.3
• UniProt Accession #: P10639; Q52KC4; Q9D8R0
• Molecular Weight: 11.9kD
• NCBI Official Full Name: thioredoxin
• NCBI Official Synonym Full Names: thioredoxin 1
• NCBI Official Symbol: Txn1
• NCBI Official Synonym Symbols: ADF; Txn; Trx1; AW550880
• NCBI Protein Information: thioredoxin; trx; ATL-derived factor
• UniProt Protein Name: Thioredoxin
• Protein Family: Thioredoxin
• UniProt Gene Name: Txn
• UniProt Synonym Gene Names: Txn1; Trx; ADF
• UniProt Entry Name: THIO_MOUSE

Uniprot Description

TXN: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity. Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA- binding activity in a redox-dependent manner. Up-regulated by ionizing radiation. Belongs to the thioredoxin family.

Protein type: Nuclear receptor co-regulator

Cellular Component: mitochondrion; cell soma; axon; dendrite; cytoplasm; extracellular region; cytosol; nucleus

Molecular Function: protein binding; enzyme binding; protein disulfide oxidoreductase activity; peptide disulfide oxidoreductase activity; oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor

Biological Process: negative regulation of protein export from nucleus; transcription, DNA-dependent; protein folding; negative regulation of transcription from RNA polymerase II promoter; positive regulation of peptidyl-serine phosphorylation; glycerol ether metabolic process; sulfate assimilation; response to radiation; regulation of transcription, DNA-dependent; transport; cell redox homeostasis; regulation of protein import into nucleus, translocation; positive regulation of DNA binding