USP28 is a deubiquitinating enzyme of the C19 peptidase family that regulates MYC stability and DNA damage response checkpoints. USP28 regulates DNA repair by deubiquitinating and thereby stabilizing CLSPN - a protein that is ubiquitinated by the APC/C E3 Ubiquitin ligase in a cell-cycle dependent manner. USP28 interacts with isoform 1 of FBXW7 in the nucleoplasm, and regulates MYC degradation by counteracting its ubiquitination. Recently, a potential role in HIF-1 alpha -dependent processes such as angiogenesis and metastasis has been described for this deubiquitinase. USP28 has been demonstrated to cleave K6, K11, K48, and K63-linked poly-Ubiquitin chains. This recombinant protein contains a C-terminal 6-His tag.