The Human Protein Atlas Program has carefully selected three different human cell lines, A-431 epidermoid carcinoma, U-251 MG glioblastoma and U-205 osteosarcoma, for organelle mapping of the proteome. As Prestige Antibodies are studied by immunofluorescence (IF) staining, three well-characterized organelle
O-Linked glycans are usually attached to the peptide chain through serine or threonine residues. O-Linked glycosylation is a true post-translational event and does not require a consensus sequence. The most common type of O-linked glycans contain an initial GalNAc residue
Post-translational modifications such as glycosylation, phosphorylation, and sulfation, to name a few, serve many functions. As a result, the analysis of proteins and their post-translational modifications is particularly important for the study of diseases where multiple genes are known to
A novel method has been developed to tag antibodies with a photoreactive iridium catalyst. Light activates the catalyst to convert a diazirine compound into a reactive carbene intermediate that can label membrane proteins in close proximity. The diazirine adds a
Phosphorylation is an important covalent post-translational modification (PTM) in cell signalling pathways. Protein phosphorylation is the reversible addition of a phosphate group to a protein or small molecule catalysed by protein kinases. Approximately one third of the 30,000 proteins encoded
This page shows how to cleave and purify GST-tagged proteins bound to Glutathione Sepharose in batch mode from Cytiva. Glutathione Sepharose High Performance, Glutathione Sepharose 4 Fast Flow, and Glutathione Sepharose 4B can all be used for cleavage and purification
Explore various strategies for deglycosylating N-linked glycans involving PNGase F, PNGase A (Glycopeptidase A), and even native and sequential deglycosylation with endoglycosidases like Endoglycosidase H, Endoglycosidase F, and exoglycosidases.
Structural modifications of proteins are essential to living cells. When aberrantly regulated they are often the basis of disease. Glycans are responsible for much of the structural variation in biologic systems, and their representation on cell surfaces is commonly called
Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the one enzyme-one linkage concept. Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some
Chiral amines have found widespread application in asymmetric synthesis serving, for instance, as chiral bases in enantioselective deprotonation reactions or being valuable substances for resolving racemic mixtures of acids.
The immune system protects the body from disease by resisting the invasion of foreign molecules into its cells, for example peptides and proteins are hydrolyzed by proteolytic enzymes; nucleic acids are hydrolyzed by nucleases; and most small molecules are eliminated
Our's GlycoProfile Beta-Elimination Kit allows researchers to perform complete glycoproteomics research by preserving both the O-glycans and protein, specifically remove o-glycans, label o-glycans prior to analysis, have confidence in uniformity of procedure. While it is known that O-glycosylation plays
Our Streptavidin HC (High-Capacity) multiwell plates are prepared with a highly-porous, high-density streptavidin coating. Streptavidin has similar biotin-binding characteristics as avidin. Streptavidin can bind 4 moles of biotin per mole of protein with high selectivity and affinity (Kd~10-15). Unlike avidin