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Tris-(2-Carboxyethyl)phosphine, Hydrochloride (TCEP)
Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by TCEP (tris-(2-carboxyethyl)phosphine). Unlike DTT (dithiothreitol), TCEP doesRead more
| Catalog Number | Quantity |
|---|---|
| T2556 | 1 g |
Catalog number T2556
Price (USD)
172.00
1 g
-
Quantity:
1 g
Price (USD)
172.00
1 g
Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by TCEP (tris-(2-carboxyethyl)phosphine). Unlike DTT (dithiothreitol), TCEP does not contain thiols and therefore usually does not need to be removed prior to thiol modification.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
FormSolid
Quantity1 g
Shipping ConditionRoom Temperature
Unit Size1 g
Contents & Storage
Store at room temperature.
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Frequently asked questions (FAQs)
TCEP, Tris Carboxy Ethyl Phosphene is an alternative sulfhydryl reducing agent for protein samples. It is an extremely potent and effective reducing agent for particularly ‘difficult' proteins. It is compatible with the Tris-Glycine gels and NuPAGE gels. It should be added to the sample buffer for these systems. 20 mM final (maximum) concentration is sufficient for samples. You may add alkylating agents, e.g. Iodine (50 mM Iodoacetic acid), to prevent re-forming of S-S bonds but it is not necessary. Do not heat because this will hydrolyze much of your sample. Instead let the sample sit for several minutes at RT and then load.
Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.
Citations & References (161)
Search citations by name, author, journal title or abstract text
Citations & References
Abstract
A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies.
Journal:Bioconjugate chemistry
PubMed ID:12236801
Site-directed mutagenesis provides a straightforward means of creating specific targets for chemical modifications of proteins. This capability enhanced the applications of spectroscopic methods adapted for addressing specific structural questions such as the characterization of partially folded and transient intermediate structures of globular proteins. Some applications such as the steady state
Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation.
Journal:Biochemistry
PubMed ID:9724530
The agouti-related protein gene (Agrp) plays an important role in body weight regulation. The mature human protein is a single polypeptide chain of 112 amino acid residues, consisting of an N-terminal acidic region and a unique C-terminal cysteine-rich domain. The disulfide structure of recombinant human AGRP was determined by chemical
Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions.
Journal:Anal Biochem
PubMed ID:10036128
'The rate at which amide hydrogens located at the peptide backbone in protein/protein complexes undergo hydrogen/deuterium exchange is highly dependent on whether the amide groups participate in binding. Here, a new mass spectrometric method is presented in which this effect is utilized for the characterization of protein/ligand binding sites. The
A synthetic lipopolysaccharide-binding peptide based on amino acids 27-39 of serum amyloid P component inhibits lipopolysaccharide-induced responses in human blood.
Journal:J Immunol
PubMed ID:9759883
'LPS-binding proteins in plasma play an important role in modifying LPS toxicity. Significant properties have already been attributed to the LPS-binding protein (LBP). It accelerates LPS toxicity as well as incorporation into high-density lipoproteins, leading to neutralization of LPS in serum. A search for other LPS-binding components in serum, using
Mass spectrometric characterization of transferrins and their fragments derived by reduction of disulfide bonds.
Journal:J Am Soc Mass Spectrom
PubMed ID:12781465
'Mass spectrometry, proteomics, and protein chemistry methods are used to characterize the cleavage products of 79 kDa transferrin proteins induced by iron-catalyzed oxidation, including a novel C-terminal polypeptide released upon disulfide reduction. Top-down electrospray ionization tandem mass spectrometry (ESI-MS/MS) of intact multiply-charged transferrin from a variety of species (human, bovine,
161 total citations