盐酸三-(2-羧乙基)膦 (TCEP)

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引用和文献 (161)

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盐酸三-(2-羧乙基)膦 (TCEP)

蛋白质中胱氨酸的二硫化物交联可由 TCEP（三-(2-羧乙基)膦）还原为半胱氨酸残基。与 DTT（二硫苏糖醇）不同，TCEP 不含硫醇，因此通常不需要在硫醇修饰前将其去除。了解更多信息

货号	数量
T2556	1 g

货号 T2556

价格（CNY)

2,027.00

添加至购物车

价格（CNY)

2,027.00

添加至购物车

蛋白质中胱氨酸的二硫化物交联可由 TCEP（三-(2-羧乙基)膦）还原为半胱氨酸残基。与 DTT（二硫苏糖醇）不同，TCEP 不含硫醇，因此通常不需要在硫醇修饰前将其去除。

仅供科研使用。不可用于诊断程序。

数量1 g

运输条件室温

Unit Size1 g

内容与储存

在室温下储存。

常见问题解答 (FAQ)

Can other reducing agents other than DTT or BME be used to reduce proteins prior to electrophoresis? For example, what about TCEP (Tris Carboxy Ethyl Phosphene)?

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.

引用和文献 (161)

引用和文献

Abstract

A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies.

Authors:Ratner V,Kahana E,Eichler M,Haas E

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 ... More

Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation.

Authors:Bures EJ, Hui JO, Young Y, Chow DT, Katta V, Rohde MF, Zeni L, Rosenfeld RD, Stark KL, Haniu M

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 ... More

Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions.

Authors:Ehring H

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 ... More

A synthetic lipopolysaccharide-binding peptide based on amino acids 27-39 of serum amyloid P component inhibits lipopolysaccharide-induced responses in human blood.

Authors:de Haas CJ, van der Tol ME, Van Kessel KP, Verhoef J, Van Strijp JA

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 ... More

Mass spectrometric characterization of transferrins and their fragments derived by reduction of disulfide bonds.

Authors:Thevis M, Loo RR, Loo JA

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, ... More

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