For BME, use a concentration of 5% (about 100 mM). For DTT, use 5-10 mM.

To prepare a 1 M DTT solution, dissolve 1.55 g of DTT powder in 10 mL of deionized water (e.g. Water, nuclease-free, #R0581).

Dithiothreitol (DTT) is a redox reagent also known as Cleland’s reagent. It is used to break down protein disulfide bonds and stabilize enzymes and other proteins. DTT is a small molecule and is an epimeric compound of dithioerythritol (DTE) These reducing reagent products are readily supplied by AG Scientific, Inc.

This product is soluble in water (50 mg/ml), yielding a clear, colorless solution. DTT is also soluble in ethanol, acetone, ethylate, chloroform, and ether. DTT solutions should be prepared fresh daily.

DTT is hygroscopic and has sensitivity to heat. Incompatible with strong oxidizing agents, and decomposes at pH >7. 8. How long is it stable if shipped at room temperature?

If DTT is kept at room temperature it will degrade/oxidize. The main role of DTT is to keep proteins in a reduced state. If the DTT was left out for more than 72 hours it is definitely too late. Also it is better to store DTT at -20C for long term storage.

DTT penetrates the insect body through the cuticle.

May be the concentration you are using was not dissolved well at the time of preparation. Recommendation to use DTT is prepare fresh one as possible, as it is not much stable in solution form & if it does not suite then storing its aliquots at -20 C is also fine. Regards…

DTT replaces in most applications the very pungent 2-mercaptoethanol. The optimal pH range for DTT is between 7.1 and 8.0, but the reagent can be used effectively at pH 6.5-9.0. DTT is well stable (longer shelf life as a powder than 2-mercaptoethanol), however stock solutions must be used immediately and any remaining solution discarded.

DTT is highly soluble in water (clear solution, OD<0.05 at 0.02M), but also in ethanol, chloroform, ether and ethyl acetate. DTT participates to disulfide exchange reactions (Zhang 1988) that drives its major applications (see below). In example DTT is used typically at 1-10mM for protein SS reduction. It readily cross biological membranes.

DTT is widely used in biochemistry works to reduce dissulfide bridges, protect biomolecules, in sample preparation, and to denature proteins before electrophoresis analysis (SDS-PAGE). DTT is frequently used to reduce the disulfide bonds of proteins and peptides.