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PE0240

Sigma-Aldrich

Plant Fractionated Protein Extraction Kit

Suitable for any plant species or tissue

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About This Item

Code UNSPSC :
41105500
Nomenclature NACRES :
NA.56

Niveau de qualité

Utilisation

sufficient for 20 extractions

Température de stockage

−20°C

Description générale

Sigma′s Plant Fractionated Protein Extraction Kit is designed specifically for use in plant bioscience to extract qualitative hydrophilic and hydrophobic proteins samples from any type of plant species or tissue for downstream proteomic applications. The protocol does not require any ultracentrifugation or aqueous polymer two-phase partitioning (APTP). The kit includes five reagents; a plant specific protease inhibitor, a specially formulated reagent to extract hydrophilic proteins and a new chaotropic reagent with increased solubilizing power to extract more hydrophobic proteins. Also included in the kit are reducing reagent Tributylphosphine (TBP) and alkylating reagent, Iodoacetamide. These reagents improve separation during isoelectric focusing and 2-D gel electrophoresis. The protease inhibitor is a mixture of protease inhibitors with broad specificity for the inhibition of serine, cysteine, aspartic, metalloproteases and aminopeptidases. The cocktail contains 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF), bestatin, pepstatinA, E-64, leupeptin, and 1,10-phenanthroline.
Following removal of polyphenolics, tannins and other interfering substances, ground plant tissue, fresh or frozen, is resuspended in a specially formulated reagent to extract hydrophilic proteins. After sequential extractions of hydrophilic proteins, addition of the chaotropic reagent provided extracts hydrophobic membrane bound proteins. Plant debris is pelleted by centrifugation and protein extract solutions are collected. The end results are qualitative fractionated protein samples, ready for downstream proteomic analysis.

Composants de kit également disponibles séparément

Réf. du produit
Description
FDS

  • Plant Protein Extraction Reagent Type 1 1 bottle

  • C0356Protein Extraction Reagent Type 4 1 bottleFDS

  • P9599Protease Inhibitor Cocktail, for plant cell and tissue extracts, DMSO solution 3 x 1FDS

  • T7567Tributylphosphine solution, 200 mM (in N-methyl-2-pyrrolidinone), liquid 3 x 0.5FDS

  • A3221Iodoacetamide, Single use vial of 56 mg 3 vial(s)FDS

Mention d'avertissement

Danger

Classification des risques

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

Organes cibles

Respiratory system

Code de la classe de stockage

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


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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Loomis, W.D.
Methods in Enzymology, 31, 528-545 null
Yinghui Ying et al.
Plant physiology, 173(1), 812-824 (2016-11-30)
Phosphate overaccumulator2 (PHO2) encodes a ubiquitin-conjugating E2 enzyme that is a major negative regulator of the inorganic phosphate (Pi)-starvation response-signaling pathway. A yeast two-hybrid (Y2H) screen in rice (Oryza sativa; Os) using OsPHO2 as bait revealed an interaction between OsPHO2
M Ferro et al.
Electrophoresis, 21(16), 3517-3526 (2000-11-18)
As a complementary approach to genome projects, proteomic analyses have been set up to identify new gene products. One of the major challenges in proteomics concerns membrane proteins, especially the minor ones. A procedure based on the differential extraction of
Wenhao Yue et al.
The Plant journal : for cell and molecular biology, 90(6), 1040-1051 (2017-02-24)
Inorganic phosphate (Pi) transporters (PTs) play vital roles in Pi uptake and translocation in plants. Under Pi sufficient conditions, PTs are degraded to prevent excess Pi accumulation. The mechanisms targeting PTs for degradation are not fully elucidated. In this study
M Cilia et al.
Journal of biomolecular techniques : JBT, 20(4), 201-215 (2009-09-02)
Protein extraction methods can vary widely in reproducibility and in representation of the total proteome, yet there are limited data comparing protein isolation methods. The methodical comparison of protein isolation methods is the first critical step for proteomic studies. To

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