Resources

Proteomics Databases



Metabolomics Databases

• • 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.

• • Phosphorylation Site Mass Spectrometry

  Protein phosphorylation is a common post-translational modification that regulates many biological processes within cells, including cell proliferation, apoptosis, and differentiation. In eukaryotes, phosphorylation primarily occurs on residues such as serine, threonine, and tyrosine, while in bacteria, proteins are mainly phosphorylated on residues such as aspartate, glutamate, and histidine.

• • How to Detect Generalization

  Ubiquitin (Ub), unlike the single group added during phosphorylation, methylation, and acetylation modification, is a small protein composed of 76 amino acids, which is widely present in eukaryotic cells and has a highly conserved sequence. Its spatial structure consists of 5 β-folds and 1 α-helix, forming the SSHSSS structure.

• • Histone Methylation Epigenomics

  Histone methylation is an important epigenetic modification that plays a critical role in gene expression, chromosome structure, and cell fate. Methylation occurs at various sites on histones, but is mainly concentrated on the lysine (Lys) and arginine (Arg) residues at the N-terminal tail.

• • What Is the Use of Proteomics Modification

  Protein is the basic functional unit that executes cellular functions, and its expression is regulated at multiple levels by the genome, epigenetics, and post-translational modifications (PTMs). Typically, proteins require different degrees of modifications after translation to fulfill their required functions. The principle of post-translational modification is to alter the biochemical properties of proteins by adding chemical groups to one or more amino acid residues, thereby regulating protein function.

• • Histone Modification Antibodies

  Histone modification antibodies are a class of antibodies specifically designed to detect specific histone modifications. These antibodies can selectively recognize and bind to chemically modified histones, such as acetylation, methylation, phosphorylation, etc. They play a crucial role in biomedical research, particularly in the fields of epigenetics and proteomics.

• • Can Blood Be Used for Histone Modification

  The feasibility of using blood samples for histone modification research is evident. Blood contains various cell types, including red blood cells, white blood cells, and platelets. For histone modification research, the focus is usually on white blood cells because they contain cell nuclei, and histones are found within the nucleus.

• • Types of Histone Modifications

  Histone modification is an important epigenetic regulatory mechanism, achieved by adding or removing various chemical groups to specific amino acid residues on histones. These modifications can influence the structure and function of chromatin, thereby regulating gene expression. To date, at least nine different types of histone modifications have been discovered.

• • Ubiquitination Sites' Role and Importance in Protein Regulation

  The ubiquitination site of a protein refers to those specific amino acid residues on the protein molecule that can covalently bind with Ubiquitin. Ubiquitin is a small protein that plays an important regulatory role in cells, particularly in protein degradation and signal transduction. Ubiquitination is a post-translational modification process where ubiquitin molecules are attached to specific sites on the target protein.