Resources

Proteomics Databases



Metabolomics Databases

• • Antibody Isoelectric Point: Protein Charge Characterization

  The detection of antibody isoelectric point (pI) is an important method for characterizing the charge distribution of proteins. The isoelectric point refers to the pH value at which a protein carries no net charge under an electric potential, i.e. the quantity of positive charges equals the quantity of negative charges.

• • Dynamic Light Scattering Analyzer Testing Steps

  The Dynamic Light Scattering (DLS) analyzer is a device used for measuring the average dynamic diameter of particles such as nanoparticles, proteins, polymers, etc. The test process usually consists of the following basic stages:

• • Antibody Thermal Stability Determination

  Antibody thermal stability determination is to ascertain the stability of an antibody during the heating process, identify its denaturation temperature (Tm), i.e., the temperature point at which the antibody begins to lose structural stability, and evaluate its long-term stability at a specific temperature. The thermal stability of an antibody directly affects its biological activity and functionality, which is crucial for drug development, diagnostic reagents, and research applications.

• • Determination of Protein Triple Helix Structure by Circular Dich

  Circular Dichroism (CD) is a technique commonly used to study protein structure, particularly suitable for measuring the relative content of α-helix, β-sheet, β-turn, and random coil structures in proteins. The triple-helix structure of proteins, especially the triple-helix structure of collagen, can also be analyzed by circular dichroism. In the triple-helix structure of collagen, each helix is composed of three polypeptide chains.

• • How to Analyze Experimental Results of Dynamic Light Scattering?

  Dynamic Light Scattering (DLS) is a common technique used for analyzing the size distribution of nanoparticles, proteins, polymers, etc., in solution. By measuring the change in light scattering intensity over time caused by the Brownian motion of particles in the sample, the particle size can be inferred.

• • Capillary Electrophoresis Analysis

  Capillary electrophoresis (Capillary Electrophoresis, CE) is a separation technique which makes use of the difference of the migration velocity of molecules or ions in liquid medium in the capillary under the action of electric field. This method is characterized by high efficiency, high resolution, and rapid analysis, and is widely used in biochemistry, molecular biology, drug analysis, and other fields.

• • How to Detect the Thermal Stability of Collagen Protein?

  Evaluating the thermal stability of collagen is a crucial step in understanding its physical and chemical properties and assessing its potential applications. Thermal stability generally refers to the ability of collagen to maintain its structure and function during the heating process.

• • Determination of Collagen Protein Content in Liquid Phase

  Collagen is an important protein that is widely present in various human tissues, such as skin, bones, muscle tendons, and ligaments. Accurate determination of its concentration is crucial for multiple fields such as biomaterial research, food industry, and pharmaceutical research.

• • The Application of Circular Dichroism in Pharmaceutical Analysis

  Circular Dichroism (CD) uses the absorption properties of optically active substances to analyze the molecular structure of drugs. It has very valuable applications in drug analysis, including:   1. Identification of Drug Stereochemistry Many drug molecules are chiral, and their activity, metabolism, and toxicity can significantly differ due to stereochemistry. CD can differentiate the different chiral forms (enantiomers) of drugs, which is critical to ensuring drug safety and efficacy.

• • Far Ultraviolet Circular Dichroism Spectroscopy

  Circular Dichroism (CD) spectroscopy is a rapid, simple, and accurate method for studying protein structure in dilute solutions. Structural analysis is carried out using the circular dichroism of proteins and the difference in the absorption of left and right circularly polarized light by asymmetric molecules.   The CD spectrum in the far ultraviolet region mainly reflects the circular dichroism of the peptide bond.