| BML-UW1010-0100 | 100 µg | 201.00 USD | ![]() |
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| Concentration: | 1mg/ml |
| MW: | Ub2: ~17.1kDa Ub3: ~25.6kDa Ub4: ~34.2kDa Ub5: ~42.7kDa Ub6: ~51.3kDa Ub7: ~59.8kDa |
| Purity: | ≥95% (SDS-PAGE) |
| Formulation: | Liquid. In 50mM TRIS-HCl, pH 8.0, containing 50mM sodium chloride. |
| Source/Host: | Produced in E. coli. |
| Long Term Storage: | -20°C |
| Use/Stability: | Stable for at least 1 year after receipt when stored at -20°C. |
| Handling: | After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. |
| Miscellaneous/General: | For use in deubiquitinylating enzyme assays and linear polyubiquitin binding studies. Linear polyubiquitin chains, in which the C-terminal Gly of one ubiquitin is conjugated to the N-terminal Met of an adjacent ubiquitin, have been shown to be assembled in vitro by the E3 ligase complex LUBAC and ubiquitin binding domains (UBDs) with a preference for linear polyubiquitin. A possible role for linear polyubiquitin modification in NF-κB pathway activation has also been reported; suggesting an important role for linear polyubiquitinylation in cellular processes in addition to that of lysine-linked polyubiquitin protein conjugation. |
| Background / Technical Information: | The post-translational modification of proteins with polyubiquitin chains occurs in a wide range of signalling pathways and is tightly regulated in order to ensure cellular homeostasis. The function, processing and ultimate fate of polyubiquitinylated proteins is thought to be determined by the nature of the linkage between adjacent ubiquitin molecules in the polyubiquitin chain. In addition to lysine-linked polyubiquitin chains, the amino terminus of ubiquitin can be used to form head-to-tail polyubiquitin chains, in which the C-terminal Gly of one ubiquitin is conjugated to the N-terminal Met of an adjacent ubiquitin. Such linear polyubiquitin chains are structurally similar to Lys63-linked polyubiquitin, despite the chemical differences between the two linkage types. Several ubiquitin polygenes are encoded in eukaryotic cells and undergo post-translational processing to generate the cellular source of free ubiquitin monomers. However, linear polyubiquitin chains have been shown to be assembled in vitro by an E3 ligase complex, known as the linear ubiquitin chain assembly complex (LUBAC), and ubiquitin binding domains (UBDs) with a preference for linear polyubiquitin have been identified in a number of proteins. A possible role for linear polyubiquitin modification in NFκB pathway activation, involving linear polyubiquitinylation of NEMO, has also been reported. Such observations suggest that linear polyubiquitin modification of proteins may play an important role in cellular processes in addition to that of lysine-linked polyubiquitin protein conjugation. Suggested uses: 1. Deubiquitinylating enzyme substrates (general/linkage specific). 2. Investigation of polyubiquitin chain recognition by and interaction with ubiquitin binding proteins. 3. Linear polyubiquitin studies. |
