S8445
SigmaMarker™
wide range, mol wt 6,500-200,000 Da
Sinônimo(s):
protein markers, protein standards
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About This Item
Produtos recomendados
Nível de qualidade
Formulário
lyophilized powder
uso
sufficient for 10-20 large gels (16 × 18 cm)
sufficient for 20-30 mini-gels (10 × 10 cm)
vial sufficient for 50-100 PhastGels
peso molecular
6,500-200,000 Da
temperatura de armazenamento
2-8°C
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Categorias relacionadas
Aplicação
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.
Outras notas
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)
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.
Reconstituição
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.
Informações legais
SigmaMarker is a trademark of Sigma-Aldrich Co. LLC
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Nº do produto
Descrição
Preços
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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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
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
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