Proteins are important performers in regulating various cellular functions, determining whether life activities can be carried out in an orderly and efficient manner, and protein translational modifications (PTMs) play a crucial role in this process. PTMs alter the chemical or structural properties of proteins through covalent addition of functional groups or proteins, hydrolytic cleavage of regulatory subunits, or degradation of entire proteins, resulting in more complex structures and diverse functions, and ultimately the fine regulation of biological functions. These modifications include phosphorylation, glycosylation, ubiquitination, acetylation, nitrosylation, methylation, succinylation, etc. PTMs play a crucial role in cell biology, disease pathogenesis and therapeutic prevention.
Post-transcriptional modifications of proteins, especially protein phosphorylation, are involved in almost all cellular activities in the body, so detection of phosphorylated proteins is essential for the study of many developmental disorders and human diseases. Phosphorylation antibodies specifically recognize phosphorylated amino acid sites. Phosphorylation antibodies can be used to distinguish between phosphorylated and non-phosphorylated forms of proteins present, and can be used for qualitative and quantitative analysis of phosphorylated proteins.
Protein methylation is also a form of post-translational modification and generally refers to the methylation of arginine or lysine in a protein sequence. Among histones, protein methylation is the most studied class. Certain histone residues can inhibit or activate gene expression through methylation, which is closely related to many diseases such as cancer, aging, and Alzheimer's disease, and it is one of the most important researches in epigenetics, so it is significant to detect methylated proteins. Methylation antibodies can specifically recognize methylated amino acid sites and can be used to distinguish between methylated and unmethylated forms of proteins and can be used for qualitative and quantitative analysis of methylated proteins.
Protein acetylation is the process of adding acetyl groups to protein lysine residues under the action of acetyltransferases and is a mechanism by which cells control gene expression, protein activity, or physiological processes. Acetylation antibodies can specifically recognize the amino acid sites of acetylation and can be used to distinguish between acetylated and non-acetylated forms of protein presence, and can be used for qualitative and quantitative analysis of acetylated proteins.
Glycosylation is the process of attaching sugars to proteins or lipids under the control of enzymes and occurs in the endoplasmic reticulum. Sugars are transferred to proteins under the action of glycosyltransferases and form glycosidic bonds with amino acid residues on proteins. Proteins undergo glycosylation to form glycoproteins. Glycosylation is an important modification of proteins and has a role in regulating protein function. According to the type of glycosidic chain, the glycosylation of mammalian proteins can be divided into three categories, i.e., the oxygen atom of the hydroxyl groups of Ser, Thr, Hpy, and Hly is used as a linkage to form the -0-glycosidic bond type. The -N-glycosidic bond type is formed by using the amide group of Asn, the α - amino group of the N-terminal amino acid, and the ω - amino group of Lys or Arg as attachment points. A GPI glycosylphosphatidylinositol anchor consisting of ethanolamine phosphate, three mannosides, glucosamine, and fibrolipids. Glycosylation antibody can specifically recognize the amino acid sites of glycosylation and can be used to distinguish between glycosylated and non-glycosylated forms of proteins present, and can be used for qualitative and quantitative analysis of glycosylated proteins.
Lysine is one of the most easily modified amino acid groups, with modifications including methylation, ubiquitination, phosphorylation, acetylation, glycosylation, and propionylation, which often play important roles in functional regulation. In 2010 the University of Chicago team reported for the first time the post-translational modification of lysine succinylation, a novel protein. Four succinyl-lysine candidate peptides from three proteins (isocitrate dehydrogenase, serine hydroxymethyltransferase, and glyceraldehyde-3-phosphate dehydrogenase A (GAPDH)) were identified, and the corresponding synthetic peptides were validated by western blot analysis, in vivo isotopic succinate labeling, MS/MS, and HPLC elution, demonstrating that the identified succinyl-lysine peptide fragments were derived from in vivo proteins. This modification can respond to different physiological environments and is evolutionarily conserved. Sixty-nine succinyl-lysine sites were identified among 14 E. coli proteins by affinity purification with an anti-succinyl-lysine antibody. The results suggest that lysine succinylation is a naturally occurring lysine modification.
Cellular metabolism provides energy and materials for all life processes. An important feature of tumor cells is their heavy reliance on glycolysis to produce large amounts of lactic acid, known as the "Warburg effect", a phenomenon that was first proposed by the German scientist Otto Warburg in 1924. Warburg effect not only exists in tumors, but also widely exists in immune cell activation, cell reprogramming and other processes.
On October 24, 2019, Professor Yingming Zhao's group at the University of Chicago (Co-I as Di Zhang and Zhanyun Tang) published a study in Nature, reporting for the first time that lactate functions as a post-translational modification of histones that plays a role in the regulation of gene transcription. This discovery is the latest breakthrough in the field, which not only helps people gain a new understanding of the function of lactate, but also prompts medical biologists to re-examine the "Wahlberg effect", a classic mechanism in tumor research. Using mass spectrometry, liquid chromatography, isotope labeling, and immunology, the researchers have identified and validated the widespread presence of lactate modifications on histone lysine in human and mouse cells.
AtaGenix offers a wide range of antibody preparation services for all types of modifications, including phosphorylation, methylation, acetylation, succinylation, lactonation, and glycosylation, etc.
1. Free antigen design: Customers only offer antigen protein sequence and modification sites.
2. Stable Peptide Synthesis technology: phosphorylation, methylation, acetylation, glycosylation, succinylation, and lactylation.
3. Reliable antibody purification technology: two rounds of affinity purification for modified and unmodified peptides.
4. Multiple antibodies/monoclonal antibodies can be freely selected.
Modified Polyclonal Preparation
Peptide Synthesis & Coupling
Small samples of unpurified antisera
Purified antibodies 3-5 mg
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Modified Monoclonal Preparation
Peptide Synthesis & Coupling
Antibody production & QC
Monoclonal antibody 2 mg
Monoclonal cell line (1-3 lines)
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