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PROTRA

Millipore

ProteoPrep® Reduction and Alkylation Kit

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

shelf life

≥1 yr (when stored at 2-8°C)

storage temp.

2-8°C

Application

The ProteoPrep Reduction & Alkylation Kit contains the necessary reagents to conveniently reduce and alkylate disulfide binds in preparation for 2D gel electrophoresis. These reagents are compatible with chaotropic extraction reagents and are conveneintly packaged to save time and increase efficiency. The kit contains five vials of both the reducing agent, tributylphosphine (TBP), and the alkylating agent, iodoacetamide.

Features and Benefits

  • Tributylphosphine is supplied safely as a 200 mM solution in N-methyl-2-pyrrolidine
  • Reduction and alkylation of protein samples increase 2D spot resolution
  • Conveniently packaged components save time and increase efficiency
  • Compatibility with chaotropic extraction reagents simplifies sample preparation

Legal Information

ProteoPrep is a registered trademark of Merck KGaA, Darmstadt, Germany

Signal Word

Danger

Hazard Classifications

Acute Tox. 3 Oral - Aquatic Chronic 3 - Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Shikha Shikha et al.
Microorganisms, 10(5) (2022-05-29)
Mitochondrial ribosomes are fundamental to mitochondrial function, and thus survival, of nearly all eukaryotes. Despite their common ancestry, mitoribosomes have evolved divergent features in different eukaryotic lineages. In apicomplexans, the mitochondrial rRNA is extremely fragmented raising questions about its evolution

Articles

The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as a method of manipulating protein levels within their samples, but the ability to accurately determine these protein amounts remains a challenge. Fortunately, over the past decade, the field of proteomics has witnessed significant advances in the area of mass spectrometry. These advances, both in instrumentation and methodology, are providing researchers with sensitive assays for both identification and quantification of proteins within complex samples. This discussion will highlight some of these methodologies, namely the use of Multiple Reaction Monitoring (MRM) and Protein-AQUA.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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