Tetra-Ubiquitin: Proteins and Enzymes
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.
Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse Ubiquitin, respectively. 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.
2 results for "Tetra-Ubiquitin Proteins and Enzymes" in Products
2 results for "Tetra-Ubiquitin Proteins and Enzymes" in Products
Tetra-Ubiquitin: Proteins and Enzymes
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.
Each human Ubiquitin monomer is 76 amino acids (aa) in length and shares 96% and 100% aa identity with yeast and mouse Ubiquitin, respectively. 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.
Will be discontinued when existing inventory is gone.
| Source: | E. coli |
| Accession #: | P0CG47.1 |
| Applications: | BA |
| Source: | E. coli |
| Accession #: | P0CG47.1 |
| Applications: | BA |
