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Recombinant Human UBB protein

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Product Overview:
Recombinant Human UBB was expressed in E. coli.
Linkage specific poly-Ubiquitin chains may be used as a substrate for in vitro reactions with deubiquitinating enzymes ("DUB's") that cleave the peptide or isopeptide linkage between adjacent Ubiquitin molecules. K63-linked tetra-Ubiquitin chains are manufactured using recombinant wild-type human Ubiquitin and linkage-specific enzymes. The use of purely enzymatic techniques avoids the potential for contaminating synthetic intermediates. This fluorogenic substrate is intended for use with deubiquitinating enzymes that are unable to use mono-Ubiquitin-Rh110 as a substrate, or enzymes with activity that is stimulated by poly-Ubiquitin chains. The substrate consists of a K63-linked tetra-Ubiquitin chain with a single rhodamine attached to the C-terminus of the proximal Ubiquitin.
E. coli
X mg/ml (X μM) in 50 mM HEPES pH 7.0, 50 mM NaCl
K63-linked tetra-Ubiquitin Rhodamine 110 is ideal for use in assays requiring fluorescent detection of deubiquitinase activity. Optimal fluorescence at pH 8.0 is monitored with excitation and emission wavelengths of 485 nm and 535 nm, respectively. Reaction conditions will need to optimized for each specific application. We recommend an initial concentration of 0.1-1 μM.
Molecular Mass:
Predicted Molecular Mass: 35 kDa
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -70 centigrade as supplied.
3 months, -20 to -70 centigrade under sterile conditions after opening.

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Optional requirements on this protein +Expand
C-fusion   N-fusion  Non-tagged
His   GST  Fc  Others
<1.0 eu/μg   <0.1 eu/μg  <0.01 eu/μg  Not required
Monomer Isolation   Dimer Isolation   Not required
>80% by SDS-PAGE   >90% by SDS-PAGE  >95% by SDS-PAGE  Others
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45-1 Ramsey Road, Shirley, NY 11967, USA
USA: 1-631-559-9269  1-631-448-7888
Europe: 44-207-097-1828
FAX: 1-631-938-8127

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