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Publication : Cloning, characterization and expression of a cDNA clone encoding rabbit ubiquitin-conjugating enzyme, E2(32k).

First Author  Sun B Year  1997
Journal  Biochim Biophys Acta Volume  1351
Issue  1-2 Pages  231-8
PubMed ID  9116038 Mgi Jnum  J:42440
Mgi Id  MGI:1095756 Doi  10.1016/s0167-4781(96)00209-6
Citation  Sun B, et al. (1997) Cloning, characterization and expression of a cDNA clone encoding rabbit ubiquitin-conjugating enzyme, E2(32k). Biochim Biophys Acta 1351(1-2):231-8
abstractText  A cDNA clone encoding rabbit E2(32k) was obtained by library screening and PCR. The cDNA contains an open reading frame coding for 238 amino acids which shows an overall identity of 81% to human CDC34, the cell cycle-related ubiquitin-conjugating enzyme. A 50% homology to yeast CDC34 within the conserved core domain was also observed. Northern blot analysis indicated that three transcripts existed in all six rabbit tissues examined but their expression levels varied over a wide range. The putative cDNA coding region was highly expressed in Escherichia coli as a his-tagged protein which was purified to homogeneity. The ability of this expressed protein to form a thiolester bond with ubiquitin showed that it was functionally active. The ability of this protein to catalyze the conjugation of ubiquitin to histone H2A and H2B was also examined.
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