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[KallR]Ubiquitin (human), (recombinant) (untagged)

 
BML-UW0205-1000 1 mg 89.00 USD
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Product Specification

Sequence:H-MQIFVRTLTGRTITLEVEPSDTIENVRARIQDREGIPPDQQ RLIFAGRQLEDGRTLSDYNIQRESTLHLVLRLRGG-OH
 
MW:~8.7 kDa
 
Source:Produced in E. coli.
 
UniProt ID:P0CG47 (UBB), P0CG48 (UBC), P62979 (RPS27A), P62987 (UBA52)
 
Formulation:Lyophilized.
 
Purity:≥95% (SDS-PAGE) (Coomassie staining)
 
Purity Detail:Purified by perchloric acid treatment of a soluble lysate, followed by gradient elution from a cation exchange column.
 
Appearance:White solid.
 
Reconstitution:Reconstitute with aqueous buffers or DMSO.
 
Shipping:Shipped on Blue Ice
 
Short Term Storage:-20°C
 
Long Term Storage:-20°C
 
Use/Stability:Store solid at –20°C for up to twelve months. Store solutions at –20°C for up to three months.
 
Scientific Background:[KallR]Ubiquitin contains no lysine, with all seven lysines present in the wild type mutated to arginine (see sequence). These mutations render ubiquitin unable to form multi-ubiquitin chains and thus provide a useful negative control for poly-ubiquitinylation experiments. The ability of [KallR]ubiquitin to form an active thioester at the C-terminus is preserved, thus enabling [KallR]ubiquitin to be transferred to the lysines of substrate proteins, as is its ability to form linear N-terminal linkages to other ubiquitin molecules. It may also be used as an ubiquitin chain terminator.
 
Technical Info/Product Notes:[KallR]Ubiquitin was expressed in E. coli from the human ubiquitin gene carrying the CGC arginine codon at positions 6, 11, 27, 29, 33, 48 and 63. The protein is 76 amino acid residues in length.
 

General Literature References

Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages: H.T. Kim, et al.; J. Biol. Chem. 282, 17375 (2007), Abstract;
Controlled synthesis of polyubiquitin chains: C.M. Pickart & S. Raasi; Methods Enzymol. 399, 21 (2005), Abstract;
The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin: F. Wu-Baer, et al.; J. Biol. Chem. 278, 34743 (2003), Abstract;
Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain: T. Arnason & M.J. Ellison; Mol. Cell Biol. 14, 7876 (1994), Abstract;

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