Kendricklabs | Protein Analysis Services

  Gel electrophoresis and SDS-PAGE are two essential techniques used to analyze biomolecules like proteins and nucleic acids. Though they are related and often used together, they have distinct characteristics and serve different purposes depending on the scientific needs of researchers. Understanding the key differences between gel electrophoresis and SDS-PAGE is vital, especially for those utilizing advanced technologies like 2D Gels . In this blog, we'll explore how gel electrophoresis differs from SDS-PAGE and how 2D Gels play a critical role in protein analysis, offered by Kendrick Labs, Inc. What is Gel Electrophoresis? Gel electrophoresis is a technique used to separate molecules based on their size, charge, or shape. The process involves placing samples, such as proteins or nucleic acids, into a gel matrix (either agarose or polyacrylamide), and applying an electric current. Molecules move through the gel at different rates depending on their properties, allowing for

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a fundamental technique in molecular biology and biochemistry for separating proteins based on their molecular weight. SDS-PAGE Analysis is essential for protein characterization, including determining protein size, purity, and quantity. Understanding the core principles of SDS-PAGE is crucial for achieving accurate and reliable results in protein research. The Basics of SDS-PAGE At its core, SDS-PAGE is designed to separate proteins by size through the application of an electric field. This technique involves several key components: sodium dodecyl sulfate (SDS), polyacrylamide gels, and an electric current. SDS-PAGE Analysis relies on these components working together to ensure that proteins are separated effectively. Sodium dodecyl sulfate (SDS) is an anionic detergent that denatures proteins and imparts a negative charge proportional to their length. This ensures that proteins migrate through the gel bas