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Documentos Principais

SRP0203

Sigma-Aldrich

Peroxiredoxin II Active human

recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)

Sinônimo(s):

PRDX2, PRP, Thioredoxin-dependent peroxide reductase 1, NKEF-B, Natural killer cell-enhancing factor B, TDPX1, Thiol-specific antioxidant 1, Thioredoxin peroxidase 1

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About This Item

Código UNSPSC:
12352200
NACRES:
NA.32

fonte biológica

human

recombinante

expressed in baculovirus infected insect cells

Ensaio

≥80% (SDS-PAGE)

Formulário

aqueous solution

atividade específica

≥149 pmol/min-μg

peso molecular

22.7 kDa

embalagem

pkg of 100 μg

concentração

>0.02 mg/mL

técnica(s)

cell based assay: suitable

nº de adesão NCBI

NM_005809

nº de adesão UniProt

P32119

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Informações sobre genes

human ... PRDX2(7001)

Descrição geral

Research area: CELL SIGNALING

Peroxiredoxin 2 (PRDX2) is a typical peroxiredoxin, with 2-cysteine (Cys), a catalytic Cys51 and a resolving cysteine Cys172. Peroxiredoxins are peroxides reducing enzymes, and 2-Cys Prx subfamily contains four members in mammals, including PRDX1-4. PRDX2 is the predominant peroxidase present in mammalian erythrocytes, and its nitrated form is present in brains of patients with early Alzheimer’s disease.

Aplicação

Peroxiredoxin II Active human has been used as a supplement in the IVM (in vitro maturation) medium for the IVM of bovine follicular oocytes.

Ações bioquímicas/fisiológicas

Peroxiredoxin-2 is a ubiquitous redox-active intracellular enzyme that acts as a redox-dependent inflammatory mediator, triggering macrophages to produce and release TNF-α (tumor necrosis factor). It may be involved in peroxidase activity and resistance to overoxidation. Its levels are elevated in several human cancer cells and tissues, including colorectal cancer (CRC) and it influences diverse cellular processes involving cells survival, proliferation and apoptosis. Prdx2 plays an essential role in regulating oxidation-induced apoptosis in CRC cells and may have potential as a therapeutic target in CRC. It may also act as a possible candidate biomarker for pancreatic cancer. Prx2 is a key regulator of invasion and metastasis in melanoma.

forma física

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20, 50% glycerol and 3 mM DTT.

Nota de preparo

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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Certificados de análise (COA)

Lot/Batch Number
70011002003
7001102003

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Effect of peroxiredoxin II on the quality and mitochondrial activity of pre-implantation bovine embryos.
Fakruzzaman M et al
Animal Reproduction Science, 159, 172-183 (2015)
Weidong Lu et al.
Molecular and cellular biochemistry, 387(1-2), 261-270 (2013-11-16)
Peroxiredoxin 2 (Prdx2) is a member of the peroxiredoxin family, which is responsible for neutralizing reactive oxygen species. Prdx2 has been found to be elevated in several human cancer cells and tissues, including colorectal cancer (CRC), and it influences diverse
Doo Jae Lee et al.
Cancer research, 73(15), 4744-4757 (2013-06-12)
In melanoma, transition to the vertical growth phase is the critical step in conversion to a deadly malignant disease. Here, we offer the first evidence that an antioxidant enzyme has a key role in this transition. We found that the
Linkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal.
Salzano S, Checconi P, Hanschmann EM, et al.
Proceedings of the National Academy of Sciences of the USA, 111(33), 12157-12162 (2014)
Lía M Randall et al.
The Journal of biological chemistry, 289(22), 15536-15543 (2014-04-11)
Peroxiredoxins (Prx) are efficient thiol-dependent peroxidases and key players in the mechanism of H2O2-induced redox signaling. Any structural change that could affect their redox state, oligomeric structure, and/or interaction with other proteins could have a significant impact on the cascade
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