Recombinant Human UBE2K/E2-25K Protein, CF
Recombinant Human UBE2K/E2-25K Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
X mg/ml (X μM) in 50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Ubiquitin-conjugating Enzyme E2K (UBE2K), also known as E2-25K, HIP2, and LIG, is a 200 amino acid (aa) protein with a predicted molecular weight of 25 kDa. Human and mouse UBE2K share 100% aa sequence identity. Similar to other Ubiquitin-conjugating (E2) enzymes, UBE2K/E2-25K contains a conserved Ubiquitin-conjugating domain but is unique in that it also has a C-terminal, non-covalent Ubiquitin binding surface termed the Ubiquitin-associated domain between aa residues 160 and 200 (1,2). UBE2K/E2-25K mediates the elongation of Lys48-linked poly-Ubiquitin chains (3).UBE2K/E2-25K catalytic activity can be modulated by the post-translational addition of SUMO at Lys14 (4). Substrates include the Huntingtin protein and the tumor suppressor RB1 (5,6). UBE2K/E2-25K is widely expressed, with highest levels found in the brain cortex and striatum, and dysregulated UBE2K/E2-25K is implicated in polyglutamine diseases and Alzheimer's disease (7-9).
- Wilson, R.C. et al. (2011) Biochem. Biophys. Res. Commun. 405:662.
- Haldeman, M.T. et al. (1997) Biochemistry 36:10526.
- Chen, Z.J. et al. (1991) J. Biol. Chem. 266:15698.
- Pickler, A. et al. (2005) Nat. Struct. Mol. Biol. 12:264.
- Kalchman, M.A. et al. (1996) J. Biol. Chem. 271:19385.
- Oh, K.J. et al. (2010) Virology 396:118.
- de Pril, R. et al. (2007) Mol. Cell. Neurosci. 34:10.
- Skibinski, G.A. & L. Boyd (2012) BMC Cell Biol. 13:10.
- Song, S. et al. (2003) Mol. Cell 12:553.
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