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anti-Peroxiredoxin-SO3, pAb

YIF-LF-PA0004 100 µl INQ
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Product Data
Synonyms PAG; PAGA; PRDX1; NKEF-A; EC=1.11.1.15; Peroxiredoxin-1; Thioredoxin Peroxidase 2; Proliferation-associated Gene Protein; Natural Killer Cell-enhancing Factor A; Thioredoxin-dependent Peroxide Reductase 2; Sulfonylated
Properties
Immunogen/Antigen Sulfonylated peptide (KLH coupled) corresponding to the active site sequence common to Human Prx 1 to 4.
Application Western Blot (1:1,000~1:5,000)
Crossreactivity Human, Mouse, Rat
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Other Product Data Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.
Origin Manufactured by AbFrontier
Product Type Polyclonal Antibody
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.

Product Description

Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at their active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Prx I to IV have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Prx I. The active site cysteine (Cys51) is oxidized to cysteine sulfenic acid (Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress condition, the sulfenic intermediate (Cys51-SOH) can be easily overoxidized to cysteine sulfinic acid (Cys-SO2H) or cysteine sulfonic acid (Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that overoxidized Prx can be reduced back to the active form during recovery after oxidative stress. Anti-Prx-SO3 antibody recognizes both sulfinic and sulfonic forms of Prx and detects overoxidized Prx enzymes in H2O2-treated cells with high sensitivity and specificity. Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-α by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation.

Product References

1) Woo H.A., et al. (2003) J. Biol. Chem. 278(48):47361-47364. (General)
2) Woo H.A., et al. (2003) Science, 300:653-656. (General)
3) Chevallet M., et al. (2003) J. Biol. Chem.278(39): 37146-37153. (General)
4) Angelika Tolle, et al.(2005) Free Radic Biol Med.38:1401-1408. (General)
5) James W. Baty, et al.(2005) Biochem. J 3 Mar Published. (General)
6) Min Hee Choi et al. (2005) Nature letters 435(19): 347-353. (General)
(6) Min Hee Choi et al. (2005) Nature letters 435(19): 347-353. (General)
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