Resources

Proteomics Databases



Metabolomics Databases

• • Edman Sequencing for Protein Analysis

  Edman sequencing is a chemical method used to determine the amino acid sequence of proteins and peptides. Developed by Pehr Edman in the 1950s, this technique revolutionized protein sequencing by allowing sequential identification of N-terminal amino acids. The fundamental principle of Edman sequencing involves the reaction of phenyl isothiocyanate (PITC) with the N-terminal amino acid under alkaline conditions, forming a cyclic intermediate. Under acidic conditions, this intermediate undergoes cleava......

• • Detection of Host Cell Proteins (HCP) Based on PRM

  Host Cell Proteins (HCP) are impurities in the form of proteins that originate from production cells during the manufacturing process of biopharmaceuticals. These impurities can potentially compromise the safety, purity, and efficacy of the final product, highlighting the critical need for their detection and quantification. In this context, we utilize Parallel Reaction Monitoring (PRM) technology for HCP detection.

• • What Are DC and CPL in Circular Dichroism

  Circular Dichroism (CD) and Circularly Polarized Luminescence (CPL) are pivotal optical techniques employed in bioscience research, offering insights into molecular structures and dynamics via interactions with circularly polarized light. This review delineates the fundamental principles and diverse applications of CD and CPL in biological sciences.

• • Antibody Extinction Coefficient Detection

  The extinction coefficient of an antibody is a crucial parameter in biochemical research. By measuring and calculating the extinction coefficient, antibodies can be quantitatively analyzed to understand their structure and function, providing strong support for scientific research. The extinction coefficient refers to the ability of an antibody solution at a certain concentration to absorb light of a specific wavelength in a sample cell of unit thickness under certain conditions. It reflects the antib......

• • Circular Dichroism Analyzes Protein Secondary Structure Content

  In the field of biochemistry, the assessment of protein secondary structure content represents a fundamental aspect of understanding protein function and stability. The secondary structure of proteins encompasses local conformations, primarily including α-helices, β-sheets, β-turns, and random coils. The unique combinations and spatial arrangements of these structures are critical determinants of the overall three-dimensional architecture and functional capabilities of proteins.

• • Classification of Circular Dichroism Spectra

  Near-UV Circular Dichroism (Near-UV CD): Near-UV CD measures spectra in the range of 250-300 nm and is mainly used to analyze the tertiary structure of proteins and interactions between subunits. In this wavelength range, the side chains of aromatic amino acids and disulfide bonds have significant absorption peaks, which can be used to study the conformational changes and interactions of proteins.

• • Can Phosphorylation Mass Spectrometry Detect Phosphorylation Sites

  Mass spectrometry-based phosphorylation analysis is a powerful technique for identifying phosphorylation sites and quantifying protein phosphorylation. Phosphorylation represents a critical post-translational modification that plays a central role in regulating numerous biological processes, such as the cell cycle, signal transduction, cell differentiation, and metabolism.

• • Considerations for Detecting Phosphorylated Proteins Using Western Blot

  Protein Phosphorylation Detection using Western Blot (WB) is a widely utilized technique in biological research for evaluating protein levels and modifications. Key considerations during the detection process include sample processing, the selection of specific antibodies, the choice of control samples, signal detection, and result interpretation.

• • Detection of the Isoelectric Point of Glycoproteins

  Glycoproteins are ubiquitous in living organisms and are complex macromolecules composed of proteins and carbohydrate moieties. The isoelectric point (pI) of a glycoprotein is the pH at which the molecule is electrically neutral in solution. This pI is typically determined through isoelectric focusing (IEF), an electrophoretic technique performed along a pH gradient. Proteins migrate through this gradient and cease movement upon reaching their pI due to the neutralization of their net charge, allowing for..

• • How Many Cells Are Needed for Glycosylation Mass Spectrometry Analysis

  The number of cells required for glycosylation mass spectrometry analysis is contingent on cell type and the sensitivity of the analysis technique. Past studies typically necessitate millions to billions of cells to obtain a sufficient quantity of glycosylated proteins. The procedures for this analysis encompass cell culture, cryopreservation, cell lysis, and protein extraction. Researchers are advised to thoroughly review pertinent experimental protocols relative to their specific experimental objectives..