(Biotin-Ahx-Ub)-(Cys-Ahx-Ub) K48 linked
a native K48 linked di-Ub, modified with biotin on the N-terminus of the distal Ub and cysteine on the N-terminus of the proximal Ub
Additional information
| Weight | 0.005 kg |
|---|---|
| Applications | |
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| 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 | |
| aliquot size |
€150.00
- Description
- Additional information
- references
Description
(Biotin-Ahx-Ub)-(Cys-Ahx-Ub) K48 linked (UbiQ-119) is a native K48 linked di-Ub which is modified with a biotin tag on the distal Ub and an N-terminal cysteine on the proximal Ub*. An aminohexanoic acid (Ahx) linker is used to create extra space for efficient access of biotin binding entities and Cys reactive reagents. The Cys residue can be modified by two methods:
1) by thiol alkylation with thiol-reactive moieties (such as maleimides and iodoacetamides)
2) by native chemical ligation using activated esters (such as thioesters and NHS esters)
Ligation via method 2 retains the thiol group of the Cys residue which could then be used for attaching another label if desired. Overall, UbiQ-119 is designed to allow for the creation of various K48 diUb based conjugates which could serve for example as DUB assay reagents when the N-termini are functionalized with fluorescent labels. This product is formed by chemical ligation.
* Met1 of the proximal Ub is replaced by norleucine
Additional information
| Weight | 0.005 kg |
|---|---|
| Applications | |
| 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 | |
| aliquot size |
El Oualid, F., et al. Chemical Synthesis of Ubiquitin, Ubiquitin-Based Probes, and Diubiquitin. Angewandte Chemie Int. Ed. 49, 10149-10153 (2010).
http://www.ncbi.nlm.nih.gov/pubmed/21117055
Faesen, A.C., et al. The Differential Modulation of USP Activity by Internal Regulatory Domains, Interactors and Eight Ubiquitin Chain Types. Chem. Biol. 18, 1550-1561 (2011).
http://www.ncbi.nlm.nih.gov/pubmed/22195557
Dikic, I., et al. Ubiquitin-binding domains – from structures to functions. Nat. Rev. Mol. Cell. Biol. 10, 659-671 (2010).
http://www.ncbi.nlm.nih.gov/pubmed/19773779
Licchesi, J.D., et al. An ankyrin-repeat ubiquitin-binding domain determines TRABID’s specificity for atypical ubiquitin chains. Nat. Struct. Mol. Biol. 19, 62-71 (2012).
http://www.ncbi.nlm.nih.gov/pubmed/22157957