Each Ubiquitin contains a Pro substitution at position 73.
UCN-312 | | |
Formulation 100 μl of agarose supplied in a 200 μl total volume of 20% Ethanol. | ||
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Do not freeze.
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With a predicted molecular weight of 34 kDa, Tetra-Ubiquitin chains are composed of four Ubiquitin monomers that are covalently linked through isopeptide bonds, which typically form between a lysine residue of one Ubiquitin molecule and the C-terminal glycine residue of another Ubiquitin molecule (1). Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse Ubiquitin, respectively (2). Seven of the 76 aa in Ubiquitin are lysine residues that can participate in poly-Ubiquitin chain formation. Linkage through specific lysine residues is thought to serve as a signal that affects protein degradation, signaling, trafficking, and other cellular processes (3-8).
Linkage specific, non-hydrolyzable tetra-Ubiquitin is resistant to the activity of deubiquitinating enzymes (DUB's) that cleave the isopeptide linkage between adjacent Ubiquitin molecules. It can be used to investigate binding interactions between tetra-Ubiquitin and proteins that contain elements such as Ubiquitin-associated domains (UBA's), Ubiquitin-interacting motifs (UIM's), and CARD domains. This product may also be useful in exploring the role of unanchored poly-Ubiquitin chains in some signaling pathways.
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