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Ubiquitin K63 Selector affinity resin - N1910

The Ubiquitin K63 Selector specifically recognizes the lysine 63 linkages in polyubiquitin and will only precipitate polyubiquitin chains when this particular linkage is present


This product was developed by NanoTag and Hybribody 



Selector resins are based on a high-affinity single-domain antibody (sdAb) that is covalently immobilized on 4 % cross-linked agarose beads.

Camelid single domain affinity resin
Cat. No.: N1910
Amount: 2000 µl
Price: $355.00
Cat. No. N1910

2000 µL slurry

Storage Store at 4 °C, do not freeze
IP: yes (see remarks)
Specificity Recognizes K63-linkage of polyubiquitins
Formulation 50 % slurry in PBS containing 20 % Ethanol
Shelf life Stable for 12 months

IP: The NanoTag IP-protocol for selector resins is a good starting point. Further optimization may be necessary.

Cat. No.: N1910
Amount: 2000 µl
Price: $355.00

Ubiquitin (Ub) is a small (8.6 kDa) regulatory protein. By conjugation of one or more ubiquitin molecules (monoubiquination or polyubiquination) almost all eukaryotic can be modified posttranslationally. modification that affects nearly all proteins in eukaryotes.Different ubiquination patterns have different effects on the tagged proteins, e.g. they can be targeted for degradation of the proteasome, their cellular localization or activity can be affected. The Ubiquitin Selector is based on a high-affinity single-domain antibody (sdAb) that is covalently immobilized on 4% cross-linked agarose beads and specifically recognizes the ubiquitin residues for immunoprecipitations. The Ubiquitin pan Selector will purify ubiquitin residues irrespective of its linkage to other subunits or its multimeric state. The Ubiquitin K48 Selector recognizes only polyubiquitin chains that have a K48 linkage, a linkage that often related to degradation of the modified protein via the proteasome. The K63 linkage of ubiquitin may regulate the endocytic trafficking of the modified protein. This linkage is specifically precipitated by the Ubiquitin K63 Selector.