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S8445

Sigma-Aldrich

SigmaMarker™

wide range, mol wt 6,500-200,000 Da

Sinónimos:

protein markers, protein standards

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About This Item

MDL number:
MFCD00165844
UNSPSC Code:
41105337
NACRES:
NA.25

Quality Level

200

form

lyophilized powder

usage

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

mol wt

6,500-200,000 Da

storage temp.

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.

Other Notes

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.

Legal Information

SigmaMarker is a trademark of Sigma-Aldrich Co. LLC

Related product

Referencia del producto
Descripción
Precios

08168

Timestrip Plus™ 8 °C

pictograms

Health hazard
GHS08

signalword

Danger

Hazard Classifications

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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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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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