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444810

Sigma-Aldrich

ProteoExtract® Native Membrane Protein Extraction Kit

Synonyme(s) :

Membrane protein extraction kit

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About This Item

Code UNSPSC :
41106500
Nomenclature NACRES :
NA.77

Utilisation

sufficient for 20 extractions

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze

Technique(s)

protein extraction: suitable

Entrée

sample type: mammalian tissue

Conditions d'expédition

ambient

Température de stockage

2-8°C

Description générale

A convenient kit for the isolation of native integral membrane and membrane-associated proteins, without the need for ultracentrifugation. Extraction is based on association of proteins with cellular membranes rather than on their hydrophobicity. Resulting samples are suitable for use in functional assays, 2-D gel electrophoresis, and other applications.
Membrane proteins represent only one-third of the proteins encoded by the human genome, but they represent more than two-thirds of the known protein targets for drugs. Therefore, approaches to prepare and characterize membrane proteins are of significant interest for drug discovery. However, due to their hydrophobic nature, membrane proteins are more difficult to analyze than soluble proteins. In addition to the intrinsic difficulty of solubilization, membrane proteins are challenging because of their general low abundance. Thus, the challenges for sample preparation of membrane proteins are effective solubilization and selective enrichment, ideally keeping proteins in a non-denatured state.
Note: 1 kit is sufficient for up to 20 sample extractions.

Composants

Wash Buffer, Extraction Buffer 1, Extraction Buffer 2, Protease Inhibitor Cocktail, and a user protocol.

Avertissement

Toxicity: Multiple Toxicity Values, refer to MSDS (O)

Principe

The ProteoExtract® Native Membrane Protein Extraction Kit is designed for the isolation of native membrane proteins from a broad range of mammalian samples, including:

• Adherent tissue culture cells

• Suspension grown tissue culture cells

• Frozen cell pellets

• Tissues

Notes préparatoires

The amount of buffer required for each extraction is dependent upon the amount of starting cell material.

Stockage et stabilité

• Wash Buffer

Store at 4°C.

• Extraction Buffers I & II

The Extraction Buffers I and II can be stored at 4°C for up to 6 month.

For prolonged storage, freeze the buffers in convenient aliquots at -20°C. Before extraction, buffers must be thawed at room temperature (RT). After thawing, mix components by gently shaking or vortexing. Avoid repeated freezing and thawing!

• Protease Inhibitor Cocktail

The Protease Inhibitor Cocktail is supplied in DMSO and can be stored at 4°C up to 6 months. For prolonged storage, freeze the cocktail in convenient aliquots at -20°C. During the sample preparation procedure it must be kept at RT to prevent freezing of DMSO.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
PROTEOEXTRACT is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Aquatic Chronic 3 - Eye Irrit. 2 - Skin Irrit. 2

Code de la classe de stockage

10 - Combustible liquids


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Consulter la Bibliothèque de documents

Wenlu Li et al.
Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism, 39(10), 2048-2060 (2018-05-23)
Blood-brain barrier (BBB) disruption in neurological disorders remains an intractable problem with limited therapeutic options. Here, we investigate whether the endothelial cell membrane protein annexin A2 (ANXA2) may play a role in reducing trans-endothelial permeability and maintaining cerebrovascular integrity after
Stefanie Bünger et al.
Cytotechnology, 61(3), 153-159 (2010-01-15)
Membrane proteins account for 70-80% of all pharmaceutical targets emphasizing their clinical relevance. Identification of new, differentially expressed membrane proteins reflecting distinct disease properties is thus of high importance. Unfortunately, isolation and analysis of membrane-bound proteins is hampered by their
Jacqueline Bezençon et al.
Journal of pharmaceutical sciences, 110(1), 404-411 (2020-10-16)
Recent studies have focused on coproporphyrin (CP)-I and CP-III (CPs) as endogenous biomarkers for organic anion transporting polypeptides (OATPs). Previous data showed that CPs are also substrates of multidrug resistance-associated protein (MRP/Mrp) 2 and 3. This study was designed to
Robyn T Sussman et al.
Frontiers in oncology, 10, 302-302 (2020-03-27)
We developed a computational pipeline designed to use RNA sequencing (n = 136) and gene expression profiling (n = 250) data from neuroblastoma tumors to identify cell surface proteins predicted to be highly expressed in MYCN amplified neuroblastomas and with
Meenakshi Upreti et al.
Journal of molecular medicine (Berlin, Germany), 91(4), 497-506 (2012-10-24)
The present study reports on a new strategy for selective, radiation therapy-amplified drug delivery using an antiangiogenic 33-a.a., tumor vasculature-targeting ligand, anginex, to improve the therapeutic ratio for strategies developed against solid tumors. Our findings indicate that galectin-1 is (a)

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