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PROTRA

ProteoPrep® Reduction and Alkylation Kit

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142,80 €

142,80 €

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Über diesen Artikel

NACRES:
NA.32
UNSPSC Code:
12352200

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shelf life

≥1 yr (when stored at 2-8°C)

storage temp.

2-8°C

Quality Level

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Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

shelf life

≥1 yr (when stored at 2-8°C)

shelf life

-

shelf life

-

shelf life

-

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

signalword

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

Lagerklasse

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

wgk

WGK 3


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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
Shinobu Takagi et al.
Bioscience, biotechnology, and biochemistry, 84(11), 2241-2252 (2020-07-23)
A simple intracellular proteomic study was conducted to investigate the biological activities of Aspergillus niger during industrial enzyme production. A strain actively secreting a heterologous enzyme was compared to a reference strain. In total, 1824 spots on 2-D gels were

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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.

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