(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

productsheet

code UbiQ-119 Category
product UbiQ-119 Category

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

Clear
View cart

150.00

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