Un reagente eccellente per impedire l′ossidazione di gruppi SH ridotti; riduce i disolfuri quantitativamente. DTT è efficace in soluzioni tampone dei campioni per ridurre i legami proteina disolfuro prima dell′SDS-PAGE. DTT può anche essere usato per ridurre il ponte disolfuro del reticolante N,N′-bis(acriloil)cistammina per scindere la matrice del gel di poliacrilammide. DTT è meno aggressivo e tossico rispetto al 2-mercaptoetanolo. Tipicamente si ricorre a una concentrazione di DTT (100 mM) sette volte più bassa rispetto al 2-mercaptoetanolo (5% v/v, 700 mM).
The Journal of biological chemistry, 288(10), 7230-7240 (2013-01-25)
In Pichia pastoris, the peroxisomal targeting signal 2 (PTS2)-dependent peroxisomal matrix protein import pathway requires the receptor, Pex7, and its co-receptor Pex20. A conserved lysine (Lys(19)) near the N terminus of Pex20 is required for its polyubiquitination and proteasomal degradation
In eukaryotes, deubiquitinases (DUBs) remove ubiquitin conjugates from diverse substrates, altering their stabilities, localizations or activities. Here we show that many DUBs of the USP and UCH subfamilies can be reversibly inactivated upon oxidation by reactive oxygen species in vitro
Environmental science and pollution research international, 20(8), 5502-5511 (2013-02-26)
Effect of nitric oxide donor (sodium nitroprusside, SNP, 500 μM) or hydrogen peroxide scavenger (dithiothreitol, DTT, 500 μM) on cadmium (Cd) or copper (Cu) uptake (150 μM solutions) and toxicity using Scenedesmus quadricauda was studied. Combined treatments (Cd or Cu
Thioredoxin (Trx) is a key player in redox homeostasis in various cells, modulating the functions of target proteins by catalyzing a thiol-disulfide exchange reaction. Target proteins of cytosolic Trx-h of higher plants were studied, particularly in the plasma membrane, because
The Journal of biological chemistry, 288(19), 13522-13533 (2013-03-29)
CXCL4L1 is a highly potent anti-angiogenic and anti-tumor chemokine, and its structural information is unknown. CXCL4L1 x-ray structure is determined, and it reveals a previously unrecognized chemokine structure adopting a novel C-terminal helix conformation. The alternative helix conformation enhances the
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