|Calculated MW||8.732 kDa|
|Storage||-80°C; 4 mg/ml in 50 mM Tris, pH 7.5, 150 mM NaCl, 10% glycerol.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Ubiquitin is a small polypeptide that can be conjugated via its C-terminus to amine groups of lysine residue on target proteins. This conjunction is referred to as monoubiquitylation. Additional ubiquitin moieties can be subsequently conjugated to this initial ubiquitin, utilizing any one of the seven lysine residues on the surface of ubiquitin. The formation of these ubiquitin chains is referred to as polyubiquitylation. This tag-free recombinant form of human ubiquitin is engineered to have all available lysines mutated to arginines, except at position 48. This molecule, therefore, can only form polyubiquitin chains of K48 linkage type. Covalent attachment of ubiquitin to other proteins serves various functions, but its major role is to target cellular proteins for destruction. Cellular components that activate, transfer, remove, or simply recognize ubiquitin number in the hundreds, perhaps even in the thousands. In light of this complexity the ubiquitin pathway is ideal for a systems biology approach. Ubiquitin plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The Ub-proteasome proteolytic pathway, which is a complex process, is implicated to be of great importance for regulating numerous cellular processes.
Pancre V.,et al.Eur. J. Immunol. 21:2735-2741(1991).
Adams S.M.,et al.Br. J. Cancer 65:65-71(1992).
Hillier L.W.,et al.Nature 434:724-731(2005).
Vladimirov S.N.,et al.Eur. J. Biochem. 239:144-149(1996).
Schlesinger D.H.,et al.Nature 255:423-424(1975).
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