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PROTMEM

Millipore

ProteoPrep® Membrane Extraction Kit

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

General description

ProteoPrep® Membrane Extraction Kit reagents utilize a powerful detergents for higher loading and resolution of proteins in 2D gels. Protein Extraction Reagent Types 3 and 4 are optimized for proteomic studies. Extraction reagents 3 and 4 are ideal for protein extraction prior to isoelectric focusing and 2D electrophoresis. This kit also includes reagents for the reduction and alkylation of disulfide bonds. The ProteoPrep® Membrane Extraction Kit was designed through a collaboration of Proteome Systems and Sigma research scientists.

Application

ProteoPrep® Membrane Extraction Kit is designed to prepare highly enriched membrane protein solutions from many types of cells. The final protein solution are suitable for 2D gel electrophoresis.

Features and Benefits

  • Innovative detergent preparations - Improved solubility allows for higher protein loads and greater visibility of low abundance proteins in 2D gels.
  • Two pre-mixed solubilization solutions - Removes interfereing non-membrane proteins prior to extractions, resulting in uncluttered 2D arrays.
  • Pre-measured reducing & alkylating reagents - Easy-to-use reagents provide improved IEF resolution.

Legal Information

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

Los componentes del kit también están disponibles por separado

Referencia del producto
Descripción
SDS
  • T7567Tributylphosphine solution, 200 mM (in N-methyl-2-pyrrolidinone), liquid 5 x 0.5SDS
  • C0356Protein Extraction Reagent Type 4 23 mLSDS
  • A3221Iodoacetamide, Single use vial of 56 mg 5 x 56SDS

signalword

Danger

Hazard Classifications

Acute Tox. 3 Oral - Aquatic Chronic 2 - Carc. 2 - Eye Dam. 1 - Repr. 1B - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3

target_organs

Respiratory system

Storage Class

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

flash_point_f

186.8 °F - closed cup

flash_point_c

86 °C - closed cup

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Medicharla Venkata Jagannadham et al.
Journal of proteomics, 75(8), 2488-2499 (2012-03-16)
Antarctic bacteria are adapted to the extremely low temperature. The transcriptional and translational machineries of these bacteria are adapted to the sub-zero degrees of temperature. Studies directed towards identifying the changes in the protein profiles during changes in the growth
Ji Youn Lim et al.
Applied and environmental microbiology, 73(7), 2037-2047 (2007-02-06)
Escherichia coli O157:H7 causes hemorrhagic colitis and hemolytic-uremic syndrome in humans, and its major reservoir is healthy cattle. An F-like 92-kb plasmid, pO157, is found in most E. coli O157:H7 clinical isolates, and pO157 shares sequence similarities with plasmids present
Fang Chen et al.
Proteomics, 7(9), 1529-1539 (2007-04-05)
Plant plasma membrane (PM) proteins play important roles in signal transduction during defense response to an attacking pathogen. By using an improved method of PM protein preparation and PM-bound green fluorescent protein fusion protein as a visible marker, we conducted
Haiqing Sheng et al.
Applied and environmental microbiology, 74(16), 5015-5022 (2008-06-17)
Escherichia coli O157:H7 causes hemorrhagic colitis and the life-threatening hemolytic-uremic syndrome in humans and transiently colonizes healthy cattle at the terminal rectal mucosa. To investigate the role of the O antigen in persistence and colonization in the animal host, we
Neal X Chen et al.
American journal of physiology. Renal physiology, 292(2), F599-F606 (2006-09-14)
Fetuin-A is a known inhibitor of vascular calcification in vitro. In arteries with calcification, there is increased immunostaining for fetuin-A. However, vascular smooth muscle cells (VSMC) do not synthesize fetuin-A, suggesting fetuin-A may be endocytosed to exert its inhibitory effects.
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