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>   首页   >   产品   >   一抗   >   代谢   >   Thioredoxin (TRX) Antibody (N-term)   

Thioredoxin (TRX) Antibody (N-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Thioredoxin (TRX) Antibody (N-term) AP1337a
    Anti-TrX Antibody (M1) at 1:1000 dilution + Hela whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 12 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 1 - Thioredoxin (TRX) Antibody (N-term) AP1337a
    Western blot analysis of anti-TrX Pab (AP1337a) in HL-60 cell line lysate. TrX(arrow) was detected using the purified Pab.
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Product info
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession P10599
Other Accession Q5T937
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 11737 Da
Additional info
Gene ID 7295
Other Names Thioredoxin, Trx, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1
Target/Specificity This Thioredoxin (TRX) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human Thioredoxin (TRX).
Dilution WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsThioredoxin (TRX) Antibody (N-term) is for research use only and 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=Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus
Research Areas

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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