Resources

Proteomics Databases



Metabolomics Databases

• • HCP Host Protein Residue

  Host cell proteins (HCP) refer to the protein components from the host cells of the production cell line in biological products, which mainly include the structural proteins and secretory proteins of the host cells. These proteins are diverse and their physical and chemical properties, such as isoelectric point, hydrophobicity, relative molecular weight, etc., often have significant differences.

• • Purity Analysis of Oligonucleotides

  Oligonucleotides are typically composed of short-chain nucleotides (deoxyribonucleotides or ribonucleotides) of less than 20, serving as short RNA and DNA oligomers. They can be used as probes to determine the structure of DNA or RNA, and are used in processes such as gene chips, electrophoresis, and fluorescence in situ hybridization.   Oligonucleotides are widely used in biology, agriculture, medicine, and other fields mainly through chemical synthesis.

• • Cell Gene Knockout Technology

  What is Gene Knockout Technology? Gene knockout (Gene Knockout) is a molecular biology technique that allows researchers to block or shut off the function of a specific gene to study its role and importance. This technique is achieved by introducing mutations into the gene, making it impossible for the gene to express properly or produce functional proteins.

• • Why Does Protein Sequencing Start at the N-Terminus?

  Degradation in protein sequencing usually starts from the N-terminus (amino terminal) mainly due to:   1. Enzyme Specificity The enzyme used for protein sequencing, such as phenyl isothiocyanate (PITC) in Edman degradation, specifically reacts with the N-terminal amino acid of the protein. This specificity ensures the accuracy and repeatability of the sequencing process.   2. Convenience of Sequencing Starting from the N-terminus, each amino acid can be removed step by step and identified.

• • Immunological Detection Method for Protein Acetylation Detection

  Acetylation is a common type of post-translational modification of proteins, which plays an important role in regulating the function and stability of proteins. Immunodetection is a commonly used method for detecting protein acetylation, including Western blot and Immunoprecipitation.

• • Detecting Disulfide Bonds in Proteins

  A disulfide bond is a stable covalent bond generated by the reduction of thionitric acid by two cysteine residues. This bond plays a key role in stabilizing the tertiary structure of proteins. The number and position of disulfide bonds determine the stability and function of proteins.

• • Polyubiquitination Detection

  Ubiquitination is a unique post-translational modification process that involves attaching a small protein of 76 amino acids, known as ubiquitin, to the target protein one by one through a three-enzyme cascade reaction (E1, E2, and E3 enzymes). This process can be repeated to form a ubiquitin chain on the ubiquitinated target protein, a phenomenon known as polyubiquitination.

• • Neutrophil Proteomics

  Neutrophil proteomics is the field of study that examines the composition and function of proteins within neutrophils (a type of white blood cell, also known as a type of leukocyte). Neutrophils are part of the immune system, playing a crucial role in eliminating infections and inflammation. By studying the proteome of neutrophils, we can gain deeper insight into their role in immune response, inflammation regulation, and disease progression. The research content of neutrophil proteomics includes:

• • Quantitative Proteomics Labeling

  With the advancement of proteomics, qualitative analysis of protein types and modifications alone can no longer meet research needs. In this context, quantitative proteomics technology has emerged and has become one of the hot topics in life sciences in recent years. The quantification technology of proteomics is based on the known protein type, and quantifies its expression and abundance based on the signal intensity given by mass spectrometry. It can be divided into targeted and non-targeted.

• • Unlabeled Quantitative Proteomics

  Label-free Quantitative Technology is one of the methods for studying quantitative proteomics. Compared to traditional labeling quantitative methods, label-free quantitative protein technology has significant advantages. Traditional labeling methods usually involve complex experimental steps, which are time-consuming and laborious, and the cost of labeling reagents is high.