Post translational modifications (PTMs) are biochemical alterations to one or more amino acids of a protein. PTMs, which occur after protein translation, can have profound effects on the protein's function, interactions, half-life, and subcellular location. Thus, PTMs expand the human proteome from ~20,000 nonmodified canonical proteins to an estimated 1 million – 1 billion different protein species1,2,3.
RayBio® products enable high throughput analyses of PTMs, including phosphorylation, glycosylation, methylation, acetylation, nitration, hydroxylation, proteolytic cleavage (e.g., caspases), and carbonylation.
Covalent addition of a phosphoryl group (-PO3-), most often to a serine, threonine, or tyrosine residue.
Covalent addition of a sugar molecule, often classified by the atom to which it binds (e.g., N-linked, O-linked).
Covalent addition of one to three methyl groups to an amino acid.
Covalent addition of an acetyl group to primary amino groups, hydroxyl groups, or sulfhydryl groups.
Covalent addition of a nitro group (-NO2) to tyrosine, tryptophan, cysteine, or methionine residues.
Covalent attachment of a hydroxyl group (-OH), which most often occurs on proline.
Formation of shorter protein chains by breaking peptide bonds.
Covalent adduction of lipid aldehydes to lysine, histidine, or cysteine.
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Simultaneously detects 55 phosphorylated human proteins in the MAPK, AKT, JAK/STAT, NFκB, and TGFβ signaling pathways.
Simultaneously detects 71 phosphorylated human receptor tyrosine kinase proteins.
Simultaneously detects the glycosylation profile of 1,000 human proteins.
RayBiotech also offers ELISA kits to measure transcription factor activity. Fast, easy, high throughput, and sensitive! Learn more here.
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