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AbVideo™ - Protein

   
  • SDS-PAGE

    SDS-PAGE is a technique used to separate proteins according to their electrophoretic mobility. SDS gel electrophoresis of samples have identical charge per unit mass due to binding of SDS results in fractionation by size, visualize the separated proteins, or process further application.

    Publish: 2010/1/14

  • GST-tagged Protein Purification

    Protein purification is a series of processes intended to isolate a single type of protein from a complex mixture. We use GST-fusion protein to purify and detect proteins of interest. The GST-fusion protein can be purified from cells via its high affinity for glutathione.

    Publish: 2010/2/8

  • Protein Quantification (Silver Staining)

    Silver staining is used to detect proteins after electrophoretic separation on polyacrylamide gels. It combines excellent sensitivity while using very simple and cheap equipment and chemicals. The procedures of silver staining are protein fixation, silver impregnation and image development.

    Publish: 2010/3/15

  • Protein Quantification (Bradford Assay)

    Bradford assay is a rapid and accurate method to determine the concentration of protein. The assay is based on the observation that the absorbance maximum for an acidic solution of Coomassie Brilliant Blue G-250 shifts from 465 nm to 595 nm when binding to protein occurs. Both hydrophobic and ionic interactions stabilize the anionic form of the dye, causing a visible color change. Within the linear range of the assay (~5-25 mg/ml), the more protein present, the more Coomassie binds.

    Publish: 2010/3/15

  • GST Enzymatic Digestion

    GST fusion proteins allow convenient affinity purification of many proteins of interest but the GST-tag may become inconvenient in various downstream applications. We use PreScission protease to digest the GST fusion proteins and the protein without GST-tag is obtained.

    Publish: 2010/3/15

  • 2D Gel Electrophoresis (8) Fluorescent Staining

    SyproRuby stain is a sensitive and convenient fluorescent stain for the detection of proteins separated by gel electrophoresis. This video demonstrates the standard procedure of fluorescent staining that includes overnight staining process and the following wash steps. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/4/8

  • Protein Quantification (BCA Assay)

    The bicinchoninic acid assay (BCA Assay) is a biochemical assay for determining the total level of protein in a solution, similar to Bradford protein assay. The total protein concentration is exhibited by a color change of the sample solution from green to purple in proportion to protein concentration, which can then be measured using colorimetric techniques.

    Publish: 2010/5/24

  • 2D Gel Electrophoresis (9) Image Capture - UV Light Box

    Besides using the laser scanner to capture the 2D gel electrophoresis image, researchers can also use a UV light box to visualize separated proteins on their 2D gels. Learn how to capture the image in this tutorial. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/4/8

  • 2D Gel Electrophoresis (6) Reduction and Alkylation

    The reduction and alkylation step is required prior to any electrophoretic step to reduce the number of false spots. Here we show you the standard process to perform this step. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/3/31

  • Wheat Germ Cell-Free Protein Synthesis - Lecture Series 1

    Lecture series 1 provides an overview on the cell-free protein expression system including the advantages and the procedures involved. Dr. Masaki Madono introduced wheat germ cell-free protein synthesis system. This system is pioneered by Professor Yaeta Endo of Ehime University, Japan. This platform is based on the eukaryotic translation apparatus of wheat germ, which has significant advantages over other commonly used protein expression systems.

    Publish: 2010/9/24

  • Wheat Germ Cell-Free Protein Synthesis - Lecture Series 3

    Lecture series 3 focuses on the robotic protein synthesizers commonly used. Dr. Masaki Madono introduced wheat germ cell-free protein synthesis system. This system is pioneered by Professor Yaeta Endo of Ehime University, Japan. This platform is based on the eukaryotic translation apparatus of wheat germ, which has significant advantages over other commonly used protein expression systems.

    Publish: 2010/9/24

  • 2D Gel Electrophoresis (9) Image Capture - Laser Scanner

    Following the gel staining step, image results of a 2D gel can be captured by using a TyphoonTM Laser Scanner to capture is shown in this AbVideo. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/4/8

  • 2D Gel Electrophoresis (1) Protein Extraction

    Pure protein is the preliminary requirement of performing successful 2D gel electrophoresis. Our scientist showed you how to extract your proteins of interest by using a protein extraction kit followed by isopropanol precipitation and acetone wash steps. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/3/25

  • 2D Gel Electrophoresis (2) Protein Quantitation

    Extracted proteins can be resuspended in rehydration buffer and quantified by using Bradford assay. This AbVideo introduces the detailed procedure of measuring the protein concentration in a solution. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/3/25

  • 2D Gel Electrophoresis (3) Sample Preparation for the First Dimension

    Learn how IEF Optimizer can be used for measuring sale content of the protein samples and calculating the suggested total voltage hour for IEF process with online program. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/3/25

  • 2D Gel Electrophoresis (5) Gel Casting

    This Abvideo demonstrates the preparation and storage procedure of gel casting. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/3/25

  • 2D Gel Electrophoresis (11) Mass Sample Preparation

    Mass Sample Preparation AbVideo focuses on the workflow of mass spectrometry before samples analysis. The entire process includes protein bands excision, organic solvent wash, in-gel digestion and peptide extraction. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/5/17

  • 2D Gel Electrophoresis (7) The Second Dimension

    A thorough demonstration on how to perform the 2nd dimension of 2D gel electrophoresis is provided in this video. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/4/8

  • 2D Gel Electrophoresis (10) Visible Staining

    In addition to the fluorescent stain, the result of the 2D gel electrophoresis can also be visualized with visible stain. This video demonstrates the step-by-step procedure using VisPROTM to detect 2D gel result on the Gel Lighting Plate. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/4/8

  • 2D Gel Electrophoresis (4) The First Dimension

    Step-by-step protocol of setting the 1st dimension experiment of 2D Gel Electrophoresis is introduced in this video. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/3/25

  • 2D Gel Electrophoresis (12) Mass Analysis

    This video shows how to use MALDI-TOF system to present mass analysis. The mass spectrometry data can be blasted with online database to identify proteins. Two-dimensional gel electrophoresis, (2-DE or 2D electrophoresis), is a form of gel electrophoresis commonly used to isolate the proteins in a sample for further characterization by mass spectroscopy. Mixtures of proteins are separated in the 1st dimension by their charge (isoelectric focusing (IEF)). Then in the 2nd dimension, proteins are separated by their size (molecular weight).

    Publish: 2011/5/17

  • Wheat Germ Cell-Free Protein Synthesis - Lecture Series 2

    Lecture series 2 discusses particularly on the bilayer translation, protein synthesis and folding mechanism. Dr. Masaki Madono introduced wheat germ cell-free protein synthesis system. This system is pioneered by Professor Yaeta Endo of Ehime University, Japan. This platform is based on the eukaryotic translation apparatus of wheat germ, which has significant advantages over other commonly used protein expression systems.

    Publish: 2010/9/24

  • His-tagged Protein Purification

    Proteins with histidine tag can be purified and detected easily because the string of histidine residues binds to several types of immobilized metal ions, including nickel, cobalt and copper, under specific buffer conditions. This video provides generic protocol to purify 6xHis-tagged protein by Nickel nitrilotriacetic (Ni-NTA) sepharose.

    Publish: 2010/10/14

  • Gelatin Zymography

    Gelatin gel zymography in analyze the MMP is now recognized as the important process in cell migration, invasion or tissue remodeling.

    Publish: 2014/3/17

  • Protein Quantification (CBR)

    Coomassie Blue R (CBR) is sensitive for protein detection in PAGE gels, and protein can be directly quantitated by colorimetric. Coomassie Blue dye binds to peptides in an acidic medium. The color change of this assay is measured at 595 or 600 nm. We calculate the protein concentration using the formula created by standards. This AbVideo displays the procedure of protein quantification by using CBR.

    Publish: 2010/2/8

  • Protein Quantification (OD280)

    Steps of quantifying protein using UV absorbance (280nm) are demonstrated. 280nm absorbance depends on the Tyr and Trp (amino acids with aromatic rings) content. A very rough protein concentration can be obtained by making the assumption that the protein sample has an extinction coefficient of 1 (1 OD = 1 mg/ml protein).

    Publish: 2010/2/8

  • SDS-PAGE Gel Preparation

    SDS-PAGE is a method used to separate proteins according to their size. This video shows you how to prepare SDS-PAGE with two layers of gel, separating gel and stacking gel.

    Publish: 2010/8/2

  • Wheat Germ Cell-Free Protein Synthesis - Lecture Series 4

    Lecture series 4 shows the reagents, kits and products that are essential for protein synthesis. Dr. Masaki Madono introduced wheat germ cell-free protein synthesis system. This system is pioneered by Professor Yaeta Endo of Ehime University, Japan. This platform is based on the eukaryotic translation apparatus of wheat germ, which has significant advantages over other commonly used protein expression systems.

    Publish: 2010/9/24

  • Wheat Germ Cell-Free Protein Synthesis - Lecture Series 5

    Lecture series 5 explicitly presents the applications can be provided by the protein synthesis system. Dr. Masaki Madono introduced wheat germ cell-free protein synthesis system. This system is pioneered by Professor Yaeta Endo of Ehime University, Japan. This platform is based on the eukaryotic translation apparatus of wheat germ, which has significant advantages over other commonly used protein expression systems.

    Publish: 2010/9/24

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