Recombinant Human Thioredoxin-dependent peroxide reductase, mitochondrial(PRDX3) CSB-EP018656HU
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(Antioxidant protein 1)(AOP-1)(HBC189)(Peroxiredoxin III)(Prx-III)(Peroxiredoxin-3)(Protein MER5 homolog)(Thioredoxin-dependent peroxiredoxin 3)
Species: (Organism)
Homo sapiens (Human)
Gene Names:
PRDX3
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
PAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPANWTPDSPTIKPSPAASKEYFQKVNQ
Expression Region:
63-256aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
25.5 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Cancer
Function:
Involvement in disease:
Relevance:
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides . Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol .
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: general properties and factors affecting PrxIII activity and oligomeric state." Cao Z., Bhella D., Lindsay J.G. J. Mol. Biol. 372:1022-1033(2007)
