Post Translational Modifications

Glycosylation is a fundamental process of the biosynthetic-secretory pathway of the ER and Golgi apparatus, involving the addition of sugar moieties to specific amino acids. This modification occurs in over half of all expressed proteins and can be categorized into groups based on the amino acid that links to the carbohydrate chain (N-, O-, C-). Each protein has the ability to be glycosylated at multiple sites, potentially with different linkages, enhancing the diversity of the proteome in a way that cannot be achieved by any other post-translational modification. Factors such as enzyme availability, amino acid sequence, and protein conformation all play a role in how glycosylation occurs. Abnormal glycosylation patterns can serve as markers for certain disease states, including cancer metastasis, diabetes mellitus, inflammatory bowel disease, systemic lupus erythematosus, and many other autoimmune conditions.

This diverse structure and complex composition also makes glycoproteins more difficult to analyze, and detection tools for glycobiology research are in limited supply. To address this challenge, RayBiotech has developed three different formats of glycobiology arrays utilizing microarray technology. The Glycan arrays, Glycome Arrays, and Lectin Arrays all utilize glass slide supports with fluorescent detection and serve as powerful tools for researchers to detect glycans and/or glycan-protein interactions.

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RayBiotech has developed 3 different formats of glycobiology profiling arrays to help researchers detect glycans and/or glycan-protein interactions. All 3 formats feature glass slide supports with fluorescent detection.

Protein acetylation is a biochemical process whereby a lysine residue on a protein is modified through the addition of an acetyl group. This modification has significant implications for the structure and function of the protein. Initially identified on histones, acetylation increases the size of the side chain, attenuates the amino group's positive charge, and elevates the protein's hydrophobicity. The effects on DNA binding, enzymatic activity, protein-protein interactions, and protein degradation are far-reaching. Acetylation can stimulate gene expression by loosening the chromatin structure and rendering DNA more accessible to transcription factors and other regulatory proteins. Disrupted acetylation has been linked to various diseases, including cancer, neurodegenerative conditions, and metabolic disorders.

RayBio® Human Protein Acetylation Antibody Arrays are designed for identifying the relative levels of acetylation of lysine in up to 1,000 different human proteins in cell lysate. Cell lysate is introduced into the wells of the antibody array glass slide. Then, a biotinylated anti-acetylated-lysine antibody is used to detect acetylated-lysine on target proteins. After incubation with a fluorescent dye-conjugated streptavidin, the slides are imaged using a laser scanner.

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Protein acylation plays a significant role in cell signaling, development, and growth by covalently modifying proteins with lipids. This modification involves the addition of an acyl group, usually a fatty acid, to an amino acid residue. This changes the protein from hydrophilic to hydrophobic at one end, making it easier to interact with membranes. Protein acylation is a crucial aspect of many cellular processes relevant to physiology and diseases such as stability, localization, protein-protein interactions, and protein-DNA interactions. Furthermore, acylation plays a regulatory role in insulin secretion and insulin response pathways. Palmitoylation, the most extensively studied acyl modification, involves the addition of palmitate (a 16-carbon fatty acid) to a cysteine, and occasionally a threonine or serine residue. Unlike other acylation events, protein palmitoylation is reversible. The rapid and dynamic cycling between palmitoylation and de-palmitoylation plays an important role in membrane anchoring and trafficking between intracellular compartments.

RayBio® Human Protein S-Acylation Antibody Arrays are designed for identifying the relative levels of S-acylation of cysteine in up to 1,000 different human proteins in various biological samples. The kits use a modified biotin-switch method to label the samples, wherein the biotin-labeled samples are added to antibody arrays, washed, and incubated with a fluorescent dye-conjugated streptavidin for imaging using a laser scanner. The arrays provide a quick and efficient way to monitor changes in protein S-acylation in experimental model systems.

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Enzymatic production of nitric oxide (NO) is widespread in cells and tissues. S-nitrosylation is a covalent modification that involves binding a nitric oxide-derived group to the thiol group of cysteine. This process is a vital component of various critical cellular mechanisms, including the regulation of ion channel activity, membrane trafficking, apoptosis, and other post-translational modifications, as well as the maintenance of cellular redox equilibrium. In recent years, it has become clear that dysregulation of S-nitrosylation also contributes to the development of various diseases, including multiple sclerosis, Parkinson's disease, cancer, sickle cell disease, and asthma.

RayBio® Human Protein S-Nitrosylation Antibody Arrays are designed for identifying the relative levels of S-Nitrosylation of cysteine in up to 1,000 different human proteins in various biological samples. The kits use a modified biotin-switch method to label the proteins in the sample. The biotin-labeled samples are then added to antibody arrays, washed, and incubated with a fluorescent dye-conjugated streptavidin for imaging using a laser scanner. The arrays provide a quick and efficient way to monitor changes in protein S-Nitrosylation in experimental model systems.

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