S8445
SigmaMarker™
wide range, mol wt 6,500-200,000 Da
Synonym(s):
protein markers, protein standards
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About This Item
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Quality Level
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)
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
Product No.
Description
Pricing
signalword
Danger
hcodes
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘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)
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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
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
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)
Hemp (Cannabis sativa L.) Protein Extraction Conditions Affect Extraction Yield and Protein Quality.
François Potin et al.
Journal of food science, 84(12), 3682-3690 (2019-11-07)
The purpose of this paper was to study the extraction conditions of hemp proteins from undelipidated press-cakes. The effects of different hydration conditions on protein recovery yield and polypeptide profile were evaluated: pH (2 to 12), ionic strength (0 to
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