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Thioredoxin (TRX) Antibody (N-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession P10599
Other Accession Q5T937
Clone Names 3121801
Peptide ID 3121801
Additional Information
Gene ID 7295
Other Names Thioredoxin, Trx, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1
Target/Specificity The synthetic peptide sequence used to generate the antibody AP1337a was selected from the N-term region of human TrX . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name TXN
Synonyms TRDX, TRX, TRX1
Function 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.
Cellular Location Nucleus. Cytoplasm Secreted. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA) (PubMed:9108029). Predominantly in the cytoplasm in non irradiated cells (PubMed:11118054). Radiation induces translocation of TRX from the cytoplasm to the nucleus (PubMed:11118054). Secreted by a leaderless secretory pathway (PubMed:1332947).
Research Areas
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Background

Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1.Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

References

Cell. Signal. 17 (8), 985-996 (2005)Redox Rep. 29 (3), 281-286 (2005)Blood 105 (4), 1598-1605 (2005)Oncogene 23 (55), 8868-8875 (2004)J. Biol. Chem. 279 (29), 30369-30374 (2004)

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$ 80.00
Cat# BP1337a
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