SDS-Page: Recombinant Human Peroxiredoxin 6 Protein [NBP1-30188] - Peroxiredoxin 6, 27.1 kDa (244aa), confirmed by MALDI-TOF with a purity of 95% by SDS - PAGE
Specific activity is >2,000 pmol/min/ug. Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for 1minute.
Source
E. coli
Protein/Peptide Type
Recombinant Protein
Gene
PRDX6
Purity
>95%, by SDS-PAGE
Applications/Dilutions
Dilutions
In vitro assay
SDS-Page
Application Notes
Use In vitro reported in scientific literature (PMID 26553463).
Theoretical MW
27.1 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using NBP1-30188 in the following applications:
Analogous biological activity in mouse tissues/cells reported in scientific literature (PMID: 23792683)
Packaging, Storage & Formulations
Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
20 mM Tris-HCl buffer (pH8.0), 20% Glycerol
Preservative
No Preservative
Concentration
1 mg/ml
Purity
>95%, by SDS-PAGE
Alternate Names for Recombinant Human Peroxiredoxin 6 His Protein
1-Cys
24 kDa protein
Acidic calcium-independent phospholipase A2
aiPLA2
aiPLA21-Cys PRX
Antioxidant protein 2
AOP2
AOP2Non-selenium glutathione peroxidase
EC 1.11.1.15
EC 1.11.1.7
EC 3.1.1.-
KIAA0106Red blood cells page spot 12
Liver 2D page spot 40
MGC46173
NSGPx
NSGPx1-Cys peroxiredoxin
p29
Peroxiredoxin 6
peroxiredoxin-6
PRDX6
PRX
Background
Peroxiredoxin 6, also known as PRDX6, is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell and can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Recombinant human peroxiredoxin 6 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.
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