Resources

Proteomics Databases



Metabolomics Databases

• • Workflow of SDS-PAGE Based Protein Purity Analysis

  Protein purity analysis is a critical task in biochemical research. SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) is a widely used method that can separate and analyze protein samples, allowing researchers to evaluate protein purity and molecular weight.

• • Advantages and Disadvantages of SDS-PAGE for Protein Separation

  Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a widely used technique in biochemistry and molecular biology for protein separation. This method uses SDS, an anionic surfactant, to denature proteins, stripping them of their native three-dimensional structures and imparting a uniform negative charge. As a result, proteins can be separated primarily by molecular weight as they migrate through the gel.

• • Principle of SDS-PAGE in Protein Purity Analysis

  SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) is a widely used technique in biochemistry and molecular biology for analyzing protein molecular weight and purity. By separating proteins within a gel matrix, SDS-PAGE provides high-resolution differentiation of protein molecular weights, making it an indispensable tool in protein research.

• • Protein Structure Levels: Amino Acid Arrangement and Function

  The "arrangement order" of proteins usually refers to the sequence of amino acid residues in the protein, which is one of the main structural features of proteins. Proteins are long chain molecules formed by the linkage of amino acids through peptide bonds, and the specific sequence of these amino acids determines the structure and function of the protein.

• • Interpreting Biotechnology: The Meaning of HCP Detection

  Host Cell Protein (HCP) detection in the field of biotechnology is a crucial task that plays a key role in ensuring the purity, quality, and safety of biological products. This article will delve into the meaning, principles, methods, applications, and importance of HCP detection in the biotechnology field.

• • Considerations of Sample Amount in Circular Dichroism Spectroscopy

  Circular dichroism spectroscopy (CD) requires relatively smaller sample amounts compared to other analytical methods. However, the specific sample amount needed depends on various factors.

• • Circular Dichroism Study of α-Helical Structures

  Circular dichroism (CD) spectroscopy is a technique particularly suited for studying protein secondary structure, including α-helices, β-sheets, and random coils. This technique is based on the differential absorption of left and right circularly polarized light by molecules, which is related to their three-dimensional structure.

• • Bioanalysis of Antibody-Drug Conjugates

  Antibody-drug conjugates (ADCs) have become a hot topic in cancer treatment research in recent years. ADCs are composed of a specific tumor antigen-targeting antibody and a highly potent cytotoxic drug connected through a stable linker. The design concept of ADCs is to utilize the high specificity of antibodies to precisely target the drug to tumor cells, thereby reducing toxicity to normal cells.

• • Circular Dichroism Spectroscopy: Sample Requirements Analysis

  Circular Dichroism (CD) spectroscopy, also known as circular birefringence spectroscopy, is a spectroscopic technique primarily used for studying the three-dimensional structure of biomolecules such as proteins and nucleic acids. It is based on the principle that molecules exhibit different degrees of absorption for left- and right-circularly polarized light.

• • Application of HPLC in Protein Purity Analysis

  Proteins play a critical role in biological research and biopharmaceuticals. The purity of proteins is a crucial factor that influences both functional studies and clinical applications. High-Performance Liquid Chromatography (HPLC), a vital analytical technique, is extensively employed in the analysis of protein purity.