Resources

Proteomics Databases



Metabolomics Databases

• • Protein Sequencing Requirements for the Sample

  The requirements for samples in protein sequencing usually include the following aspects: 1. Sample Purity The purity of the protein in the sample is crucial. Excessive impurities may interfere with the sequencing results, so various methods (such as centrifugation, filtration, purification, etc.) are usually needed to enhance the purity of the protein.   2. Sample Quantity Different protein sequencing techniques require different amounts of sample.

• • Recombinant Collagen Molecular Weight

  Recombinant collagen is a type of collagen protein expressed in microorganisms, animal cells, or plants through genetic engineering technology. Compared with collagen extracted from natural sources, recombinant collagen has better safety, purity, and controllability, thus it is widely used in the biomedical and cosmetics industries. The molecular weight of recombinant collagen is an important parameter for understanding its structure and function.

• • Can Paraffin Sections Be Sent for Proteomic Sequencing?

  Paraffin sections can be used for proteomic research, but this requires special processing methods. Paraffin sections are usually used for the preservation of tissue samples, which can be used for subsequent DNA, RNA, and protein analysis. However, paraffin itself interferes with protein analysis, so the paraffin needs to be removed before proteomic analysis.

• • Is DDA Considered as Untargeted Quantitative Proteomics?

  DDA (Data-Dependent Acquisition) is one of the methods of non-labeled quantitative proteomics. In proteomic research, quantitative methods are roughly divided into two categories: labeled quantification and non-labeled quantification. DDA is a commonly used non-labeled quantitative method that relies on the data-dependent mode of the mass spectrometer to select specific precursor ions for further fragment analysis.

• • What Is the Specification for Protein Quantification Label?

  Protein quantitative tags, such as Tandem Mass Tag (TMT) and Isobaric Tags for Relative and Absolute Quantitation (iTRAQ), are chemical labels used in mass spectrometry analysis. They allow the simultaneous quantitative comparison of protein expression in multiple samples. These tags are covalently attached to peptides in the sample and detected and quantified during mass spectrometry analysis by releasing a reporter ion.

• • Ubiquitination Detection Methods

  Ubiquitination is an important post-translational modification process of proteins, involving the covalent attachment of ubiquitin proteins to substrate proteins. This process is crucial for regulating protein degradation, signal transduction, cell cycle control, and various biological functions.

• • Predict Ubiquitination Sites

  The prediction of ubiquitination sites is an important task in bioinformatics and molecular biology research. It involves predicting which sites in a protein sequence will be ubiquitinated. Ubiquitination is a post-translational modification process that involves covalently attaching ubiquitin (a small regulatory protein) to lysine residues in the target protein.

• • Recombinant Protein Glycosylation Analysis

  Recombinant protein glycosylation analysis technique is a technique used to detect and analyze the structure and composition of glycan chains in recombinant proteins. Glycosylation is a common post-translational modification process of proteins that has important effects on protein stability, activity, and intercellular interactions. Recombinant protein glycosylation analysis is particularly important in the biopharmaceutical industry as it ensures the quality and efficacy of biopharmaceutical products.

• • Silac Labeling Quantification of Histone Modifications

  SILAC (Stable Isotope Labeling by Amino acids in Cell culture) labeling is a mass spectrometry (MS) based proteomics technique used for quantitative comparison of protein expression and protein modifications under different conditions. This technique is particularly suitable for studying dynamic changes in post-translational modifications of proteins, such as phosphorylation, ubiquitination, acetylation, etc.

• • Anion-Cation Exchange Column for Glycoprotein Protein Detection

  Since the late 1940s, Ion Exchange Chromatography (IEC) technology has been widely used in protein separation operations. To date, ion exchange is still the most commonly used mode for separating proteins, including antibodies and other large biomolecules. The principle of protein separation by IEC is based on the different net charges of protein components. It separates proteins based on the different electrostatic forces between proteins and charged solid phases.