Tris (2-carboxyethyl) phosphine (TCEP) is very effective in cleaving disulfide bonds in aqueous solution. It dissolves in water and is odorless, unlike other trialkylphosphines (tributylphosphine). It is also less toxic than 2-mercaptoethanol. These advantages make it better than the other reducing agents.
It belongs to the trialkylphosphine class.
Tris (2-carboxyethyl) phosphine (TCEP) can be used in several downstream applications including SDS-PAGE, mass spectrometry, labeling with cysteine specific tags, and modification of cysteine containing compounds. It prevents oxidation of protein samples, which makes it a useful buffer component as it helps to preserve enzymatic activity. It has been used in the reduction and measurement of glutathione.
Tris (2-carboxyethyl) phosphine (TCEP) has also been used:
- to cleave cysteine residues in a synthetic peptide
- in reduction buffer for RNA Sequential Probing of Targets (SPOTs) imaging
- for the reduction of oligonucleotides
- as reducing agent during mitochondrial isolation
10×1 mL in ampule
Tris(2-carboxyethyl)phosphine hydrochloride solution reduces the disulfide bonds and leaves other functional groups intact in proteins.
As a non-mercaptan reducing agent, it avoids the toxicity inherent in thiol-containing compounds. It is capable of disrupting the botulinum neurotoxin B heavy-chain/light-chain complex that is held together by a single disulfide bond, and that is responsible for endocytosis, and ultimately the toxicity, of the toxin. Since disulfide-coupled subunits are characteristic of many toxins (e.g., ricin, snake venom, and all BoNT serotypes), it may be useful as a rescue prophylactic in cases of toxin administration.