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S8445

Sigma-Aldrich

SigmaMarker™

wide range, mol wt 6,500-200,000 Da

Synonyme(s) :

protein markers, protein standards

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About This Item

Numéro MDL:
MFCD00165844
Code UNSPSC :
41105337
Nomenclature NACRES :
NA.25

Niveau de qualité

200

Forme

lyophilized powder

Utilisation

sufficient for 10-20 large gels (16 × 18 cm)
 sufficient for 20-30 mini-gels (10 × 10 cm)
1 vial sufficient for 50-100 PhastGels

Poids mol.

6,500-200,000 Da

Température de stockage

2-8°C

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Application

SigmaMarker has been used as a protein marker in sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE).
SigmaMarkers are designed for use with Laemmli SDS-PAGE, the PhastSystem (Pharmacia) and Schagger and von Jagow SDS-PAGE (Tricine). SigmaMarkers cover the range of molecular weights common to most proteins or their subunits. The wide, high and low range markers are lyophilized with sample buffer so that they are ready-to-use after reconstitution with deionized water. The markers are formulated to yield a distribution of well-defined bands of approximately equal intensity after electrophoresis and Coomassie blue staining.

Autres remarques

Protein (mol. wt.)
Aprotinin, bovine lung (6,500)
α-Lactalbumin, bovine milk (14,200)
Trypsin inhibitor, soybean (20,000)
Trypsinogen, bovine pancreas (24,000)
Carbonic anhydrase, bovine erythrocytes (29,000)
Glyceraldehyde-3-phosphate dehydrogenase, rabbit muscle (36,000)
Ovalbumin, chicken egg (45,000)
Glutamic dehydrogenase, bovine liver (55,000)
Albumin, bovine serum (66,000)
Phosphorylase B, rabbit muscle (97,000)
β-Galactosidase, E. coli (116,000)
Myosin, porcine heart (200,000)
Will yield 12 protein bands with Coomassie Blue staining.

Reconstitution

Reconstitution with 100 μl of deionized water results in a solution containing 2-3.5 mg of protein per ml of 62 mM Tris-HCl, pH 6.8, 1 mM EDTA, 4% sucrose, 10 mM TCEP, 2% SDS, and 0.01% bromophenol blue.

Informations légales

SigmaMarker is a trademark of Sigma-Aldrich Co. LLC

Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

08168

Timestrip Plus™ 8 °C

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H315,H317,H319,H334

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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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

Thermal denaturation of pea globulins (Pisum sativum L.)-molecular interactions leading to heat-induced protein aggregation.
Mession JL, et al.
Journal of Agricultural and Food Chemistry, 61, 1196-1204 (2013)
Blanca Areli Mondaca-Navarro et al.
Journal of the science of food and agriculture, 100(7), 3228-3235 (2020-02-29)
Protein glycation by Maillard reaction is commonly used to improve the functional and bioactive properties of food proteins. It is also known that this glycation method can be accelerated by heat without the need for chemical reagents that could be
Natalia Bourguignon et al.
Ecotoxicology and environmental safety, 175, 19-28 (2019-03-18)
In the present study the polycyclic aromatic hydrocarbon removal and metabolic adaptation of Amycolatopsis tucumanensis DSM 45259 were investigated. Analysis of one-dimensional gel electrophoresis of crude cell extracts revealed differential synthesis of proteins which were identified by MALDI-TOF. To elucidate
I Berrazaga et al.
Journal of dairy science, 102(2), 1066-1082 (2018-11-26)
Food formulation and process conditions can indirectly influence AA digestibility and bioavailability. Here we investigated the effects of formulation and process conditions used in the manufacture of novel blended dairy gels (called "mixed gels" here) containing fava bean (Vicia faba)
Mehtap Çelik et al.
Journal of food science and technology, 56(6), 3023-3032 (2019-06-18)
The aims of this research were to examine the effect of pH on extraction of proteins from sour cherry (Prunus cerasus L.) kernels, and to investigate the functional properties of the resulting protein concentrate. The optimum pH values for the
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