Protein Post-translational Modification Analysis

Creative Proteomics offers a platform for the analysis of various post-translational modifications. Post-translational modifications are key mechanisms to increase proteomic diversity. Protein post-translational modifications play a key role in many cellular processes such as cellular differentiation, protein degradation, signaling and regulatory processes, regulation of gene expression, and protein-protein interactions. These modifications include phosphorylation, glycosylation, ubiquitination, nitrosylation, methylation, acetylation, lipidation and proteolysis and influence almost all aspects of normal cell biology and pathogenesis. Therefore, identifying and understanding PTMs is critical in the study of cell biology and disease treatment and prevention.

Protein post-translational modification (PTM) increases the functional diversity of the proteome by the covalent addition of functional groups or proteins, proteolytic cleavage of regulatory subunits or degradation of entire proteins. These modifications include phosphorylation, glycosylation, ubiquitination, nitrosylation, methylation, acetylation, lipidation and proteolysis and influence almost all aspects of normal cell biology and pathogenesis. Therefore, identifying and understanding PTMs is critical in the study of cell biology and disease treatment and prevention.

Protein post translational modifications may happen in several ways. Some of them are listed below: glycosylation, addition of a glycosyl group to either asparagine, hydroxylysine, serine, or threonine; acetylation, the addition of an acetyl group, usually at the N-terminus of the protein; alkylation, the addition of an alkyl group; methylation, the addition of a methyl group, usually at lysine or arginine residues; biotinylation, acylation of conserved lysine residues with a biotin appendage; glutamylation, covalent linkage of glutamic acid residues to tubulin and some other proteins.; glycylation, covalent linkage of one to more than 40 glycine residues to the tubulin C-terminal tail of the amino acid sequence.

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