|Application ||WB, IHC-P, IF|
|Other Accession||P35704, Q61171, Q2PFZ3, Q8K3U7, Q9BGI3|
|Reactivity||Human, Mouse, Rat|
|Predicted||Hamster, Monkey, Bovine|
|Calculated MW||H=22;M=22;Rat=22 KDa|
|Antigen Region||169-198 aa|
|Other Names||PRDX2; NKEFB; TDPX1; Peroxiredoxin-2; Natural killer cell-enhancing factor B; PRP; Thiol-specific antioxidant protein; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1|
|Target/Specificity||This PRDX2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 169-198 amino acids from the C-terminal region of human PRDX2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain 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.|
|Precautions||PRDX2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons 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-alpha by regulating the intracellular concentrations of H(2)O(2).|
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Provided below are standard protocols that you may find useful for product applications.
PRDX2 is a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. This protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. The crystal structure of this protein has been resolved to 2.7 angstroms.
Engstrom,K.S., et.al., Mutat. Res. (2009)
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