All chemicals were of the highest purity available and purchased from Sigma Aldrich (St. Louis, MO) or Merck (Darmstadt, Germany) unless otherwise stated. Molecular mass marker and Bio-Safe Coomassie stain for sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) were purchased from BioRad (Hercules, CA).
Molecular mass marker
Manufactured by Bio-Rad
Sourced in United States
Molecular mass markers are laboratory tools used to determine the molecular weights of proteins or other macromolecules in samples. They provide a reference standard for comparison during electrophoresis or chromatographic separation techniques.
Automatically generated - may contain errors
Lab products found in correlation
Coomassie brilliant blue r 250, by Bio-Rad (2 mentions)
Myimageanalysis software, by Thermo Fisher Scientific (1 mentions)
Coomassie blue r 250, by Bio-Rad (1 mentions)
Bsm type 1 s, by Merck Group (1 mentions)
Vertical mini gel apparatus, by Bio-Rad (1 mentions)
Image lab 5, by Bio-Rad (1 mentions)
Sds page, by Thermo Fisher Scientific (1 mentions)
Chemidoc mp, by Bio-Rad (1 mentions)
Azurespot analysis software, by Azure Biosystems (1 mentions)
7 protocols using molecular mass marker
1
SDS-PAGE Reagent Preparation
2
Protein Content and SDS-PAGE Analysis
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Quantification of proteins: The protein content of the venom was estimated by the Bradford method, as modified by Spector (1978) , using bovine serum albumin as the standard.
Electrophoresis-SDS PAGE: Electrophoresis was performed in 15 % polyacrylamide vertical minigels in the presence of sodium dodecylsulfate (SDS-PAGE) (Laemmli, 1970) . For each run, 15 μg of venom equivalent to 11 μg of protein were used under reducing conditions with β-mercaptoethanol, and 150 V were applied for 70 min in a Mini-Protean II chamber from Bio-Rad (Richmond, CA, USA). The reference venom (pool of the four regions) and venoms from each region were run in parallel with a molecular mass marker (Bio-Rad-catalog No. 161-0304). After separation, gels were stained with Coomassie Brilliant Blue. Densitometry was performed using myImageAnaly-sis™ Software from Thermo Fisher Scientific.
Electrophoresis-SDS PAGE: Electrophoresis was performed in 15 % polyacrylamide vertical minigels in the presence of sodium dodecylsulfate (SDS-PAGE) (Laemmli, 1970) . For each run, 15 μg of venom equivalent to 11 μg of protein were used under reducing conditions with β-mercaptoethanol, and 150 V were applied for 70 min in a Mini-Protean II chamber from Bio-Rad (Richmond, CA, USA). The reference venom (pool of the four regions) and venoms from each region were run in parallel with a molecular mass marker (Bio-Rad-catalog No. 161-0304). After separation, gels were stained with Coomassie Brilliant Blue. Densitometry was performed using myImageAnaly-sis™ Software from Thermo Fisher Scientific.
3
Isolation and Fractionation of Nuclear Extracts from Drosophila Embryos
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Nuclear extracts from 6- to 18-h embryos were prepared as described previously [58 (link)] with small modifications. Embryos from Oregon R were collected from apple juice plates and aged 10 h at room temperature. The extraction was completed with the final concentration of KCl at 360 mM. Fractionation of the nuclear extracts derived from 6- to 22-h embryos was performed by size exclusion chromatography using Superose 6 10/330 GL column (GE Healthcare). Molecular mass markers ranging from 1,350 to 670,000 Da (Bio-Rad) were used as gel filtration standards.
4
Characterization of BSM (Type I-S) Purity
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BSM (Type I-S) was purchased from Sigma-Aldrich (St. Louis, MO, USA). The purity was evaluated with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using a 12% polyacrylamide gel, as previously described [16 (link)]. Molecular mass markers were purchased from Bio-Rad Laboratories (Hercules, CA, USA), and the gel was stained with Coomassie blue R-250.
5
Protein Separation by SDS-PAGE
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Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed using a 5%–20% precast e-PAGEL gel (ATTO, Tokyo, Japan). After electrophoresis, the gel was stained with Coomassie Brilliant Blue R-250. The molecular weights of the protein bands in the gel were estimated using molecular mass markers (Bio-Rad Laboratories, Hercules, CA).
6
Protein Quantification and Separation
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Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed on a 12% polyacrylamide gel on a vertical mini-gel apparatus (Bio-Rad, Canada). Molecular mass markers were obtained from Bio-Rad. Proteins were stained with Coomassie Brilliant Blue R250 (Bio-Rad, Canada).
The concentration of LipY8p was determined by the Bradford assay [21 (link)], from the absorption at 595 nm, using bovine serum albumin as a standard. The optical density was measured with a UV/Vis spectrophotometer (UV70, Beckman Coulter, USA).
The concentration of LipY8p was determined by the Bradford assay [21 (link)], from the absorption at 595 nm, using bovine serum albumin as a standard. The optical density was measured with a UV/Vis spectrophotometer (UV70, Beckman Coulter, USA).
7
Proteomic Analysis of Salivary Proteins
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