protein

Peroxiredoxin-1 protein, Human (P. pastoris, His)

HY-P790010

10 μg;50 μg

60;180 USD

Peroxiredoxin-1 protein, Human (P. pastoris, His)

proteins

P. pastoris

10 μg;50 μg

60;180 USD

Peroxiredoxin-1 (PRDX1) is a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides and plays a crucial role in cellular protection against oxidative stress. It detoxifies peroxide and senses hydrogen peroxide-mediated signaling events. Peroxiredoxin-1 protein, Human (P. pastoris, His) is the recombinant human-derived Peroxiredoxin-1 protein, expressed by P. pastoris , with C-6*His labeled tag. The total length of Peroxiredoxin-1 protein, Human (P. pastoris, His) is 199 a.a., with molecular weight of ~22.1 kDa.

Human

Peroxiredoxin-1 (PRDX1), a thiol-specific peroxidase, serves as a catalytic agent in the reduction of hydrogen peroxide and organic hydroperoxides, converting them into water and alcohols, respectively. Its crucial role in cellular protection against oxidative stress involves detoxifying peroxides and acting as a sensor for hydrogen peroxide-mediated signaling events. PRDX1 may also contribute to the signaling cascades initiated by growth factors and tumor necrosis factor-alpha, potentially influencing intracellular H(2)O(2) concentrations. Notably, PRDX1 exhibits the ability to reduce an intramolecular disulfide bond in GDPD5, modulating GDPD5's capacity to drive postmitotic motor neuron differentiation. These multifaceted functions underscore PRDX1's intricate involvement in redox signaling and cellular differentiation processes.

PRDX1; PAG; OSF3; Paga; PrxI; TDX2; TPxA; prx1; MSP23

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS.

Room temperature in continental US; may vary elsewhere.