
K29 linked di-ubiquitin
isopeptide K29 linked di-ubiquitin
code
UbiQ-016
Category di-ubiquitin chains
product
UbiQ-016
Category di-ubiquitin chains
Additional information
| Weight | 0.025 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, NMR, Phenotypic protein profiling, Compound library screening |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Powder at −20°C; solution at −80°C. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
€210.00
- Description
- Additional information
- references
Description
UbiQ-016 is native K29 linked di-ubiquitin which can be used as a substrate for proteases that cleave the isopeptide linkage between two ubiquitin proteins. It can also be used to investigate mechanism of binding and recognition by proteins that contain ubiquitin-associated domains or ubiquitin-interacting motifs (UIMs). This product is formed by chemical ligation.
Additional information
| Weight | 0.025 kg |
|---|---|
| aliquot size | |
| Applications | Crystallization, NMR, Phenotypic protein profiling, Compound library screening |
| target | |
| source | |
| shipping | |
| purity | |
| molecular weight | |
| storage | Powder at −20°C; solution at −80°C. Please avoid multiple freeze/thaw cycles. |
| sample preparation | For detailed sample preparation see product sheet. |
| regulatory statement |
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El Oualid et al. Chemical Synthesis of Ubiquitin, Ubiquitin-Based Probes, and Diubiquitin. Angewandte Chemie Int Ed 2010, 49, 10149: http://www.ncbi.nlm.nih.gov/pubmed/21117055
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Faesen et al. The Differential Modulation of USP Activity by Internal Regulatory Domains, Interactors and Eight Ubiquitin Chain Types. Chem Biol 2011, 18, 1550: http://www.ncbi.nlm.nih.gov/pubmed/22195557
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Dikic et al. Ubiquitin-binding domains – from structures to functions. Nat Rev Mol Cell Biol 2010, 10, 659: http://www.ncbi.nlm.nih.gov/pubmed/19773779
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Licchesi et al. An ankyrin-repeat ubiquitin-binding domain determines TRABID’s specificity for atypical ubiquitin chains. Nat Struct Mol Biol 2012, 19, 62: http://www.ncbi.nlm.nih.gov/pubmed/22157957
