Resources

Proteomics Databases



Metabolomics Databases

• • Average Molecular Weight of Collagen Peptides

  Collagen peptides are a type of small molecule peptide obtained from collagen through enzymatic hydrolysis or other methods. They typically possess a lower molecular weight, which is beneficial for human absorption. The average molecular weight of collagen peptides usually falls within the range of 1000 to 5000 daltons (Da), although this range can vary depending on the production process and the specific requirements of the product.

• • Overview of FT-IR Analysis Technology

  FT-IR analysis, or Fourier Transform Infrared Spectroscopy, is an analytical chemistry technique used to obtain the infrared spectrum of a substance. This technique is primarily used to identify chemical substances or detect the presence of specific compounds.   FT-IR analysis is based on the ability of substance molecules to absorb infrared light at specific wavelengths.

• • 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.