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June 26, 2019

Laboratory Techniques

Affinity Chromatography Protocol

Introduction Affinity chromatography is a versatile separation protocol that uses the biological interactions for characterization and detailed analysis of sample components. It is based on highly specific interactions between two molecules, such as the interactions between enzyme and its substrate, receptor, and ligand, or antibody and antigen. These reversible interactions are used for the purification by placing one of the
Laboratory Techniques

BRADFORD Protein Determination Protocol

[divider line_type="Full Width Line" line_thickness="3" divider_color="default" animate="yes" custom_height="3" delay="100"]Do you need laboratory equipment?[divider line_type="No Line" custom_height="4"]Use the button below![divider line_type="No Line" custom_height="8"][nectar_btn size="jumbo" open_new_tab="true" button_style="regular" button_color_2="Accent-Color" icon_family="none" text="Browse Lab Equipment" url="https://conductscience.com/lab/"][divider line_type="Full Width Line" line_thickness="3" divider_color="default" animate="yes" custom_height="3" delay="100"]Introduction and Principle Developed by Marion M. Bradford in 1976, the Bradford assay is quick protocol, and the same amount of proteins
Laboratory Techniques

Fast protein liquid chromatography (FPLC) Protocol

Introduction Fast protein liquid chromatography (FPLC) is a type of liquid chromatography that provides high resolution by small-diameter stationary phases for protein characterization and separation. The technique features high loading capacity, biocompatible buffer systems, fast flow rates, and stationary phases for common chromatography modes (e.g., gel filtration, ion exchange, reversed phase, and affinity chromatography). The system enables reproducible separation by
Filtration Chromatography Protocol
Laboratory Techniques

Gel Filtration Chromatography Protocol

Introduction Gel-filtration chromatography, also known as the size exclusion chromatography, is a versatile technique that permits the separation of proteins and other biological molecules. The gel filtration chromatography separates the proteins solely based on molecular size differences. For this, a porous matrix is used to which the molecules, for steric reasons, have different degrees of access. The matrix is enclosed
Laboratory Techniques

Ion-exchange Chromatography Protocol

Introduction Ion Exchange Chromatography (IEC) is a powerful liquid chromatographic technique used for bioseparation. The separation is done by a reversible interaction between charged molecules of the sample with charged ligands attached to a column. The method offers a sizeable sample-handling capacity, powerful resolving ability, broad applicability, moderate cost, and the ease of handling. These characteristics have made the ion-exchange
Laboratory Techniques

High performance liquid chromatography (HPLC) Protocol

Introduction High-performance liquid chromatography (HPLC) is a powerful separation technique used for the analysis of ions, proteins, and organic molecules. HPLC is based on the mechanisms of adsorption, partition and ion exchange, which depend on the type of stationary phase used. The technique involves a solid stationary phase, usually enclosed in a stainless-steel column, and a liquid mobile phase. The
Laboratory Techniques

KJELDAHL Method Protocol

Introduction and Principle The Kjeldahl method was developed by a brewer called Johann Kjeldahl in 1883. The protocol is built on the principle that strong acid helps in the digestion of food so that it releases nitrogen which can be determined by a suitable titration technique. By observing the nitrogen concentration of the food, the amount of protein present is
Protein Quantification Protocols
Laboratory Techniques

Protein Quantification Protocols

Introduction: Quantitative Method The estimation of proteins via the quantitative method is one of the basic requirements in biochemistry. Proteins, from various perspectives, are substantially more complex than nucleic acids. Thus, it has been hard to give laboratory protocols that can be applied to proteins. The precise quantitation of the amount of protein during the steps of protein preparation is
SDS-Polyacrylamide Gel Electrophoresis at Neutral pH (NuPAGE)
Laboratory Techniques

SDS-Polyacrylamide Gel Electrophoresis at Neutral pH (NuPAGE)

Introduction and Principle The traditional Laemmli system denaturing conditions are stimulated by the Invitrogen NuPAGE SDS-PAGE gel system which is a revolutionary high-performance polyacrylamide gel electrophoresis system. NuPAGE gels use a unique buffer formulation to maintain a neutral operating pH during electrophoresis, which minimizes protein modifications that can result in poor band resolution. Gels are available in two formulations; Invitrogen
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Podcast

Conduct Science Podcast: Climate Change

[nectar_btn size="jumbo" button_style="regular" button_color_2="Accent-Color" icon_family="fontawesome" url="#player" text="Listen Now!" icon_fontawesome="fa fa-headphones"] Climate Change – Timestamps 00:00 – Intro 01:00 – Factoids 04:40 – Climate change denial 07:13 – What is climate change? 11:55 – Global water crisis 22:16 – Climate change and politics 27:50 – Individualistic views on climate change 32:05 – Geoengineering morality and methods 43:26 – Big companies going