The human SQSTM1/p62 is a scaffold protein which binds different substrates through its various structural motifs and therefore plays an important role in several metabolic pathways in the human body. Particularly, damaged polyubiquitinated signaling proteins are bound intracellularly by SQSTM1/p62 and proapoptotic and prosurvival pathways are activated. Moreover, SQSTM1/p62 is involved in TNF-? signaling and the activation of the transcription factor NF-?B by linking RIP to PKC? and IKK-?. Additionally, it promotes polyubiquitination of TRAF6. The protein SQSTM1/p62 therefore represents a central hub in cellular signaling pathways. In severe liver damages, i.e. alcoholic (ASH) and nonalcoholic steatohepatitis (NASH), and several neurodegenerative disorders, like Parkinson?s or Alzheimer?s disease, SQSTM1/p62 can be found together with ubiquitin in protein aggregates within the cell, because there is no autophagy occurring in these cases. In NASH, SQSTM1/p62 depicts a component of cytoplasmatic inclusion bodies, called Mallory-Denk bodies, which are formed in hepatocytes. The aim of this study was to clone the human SQSTM1/p62 cDNA into a suitable vector for heterologous expression of the protein in E. coli and its purification for subsequent NMR structure studies in order to identify binding domains and potential binding partners of SQSTM1/p62 in Mallory-Denk bodies and for redox-characterization of the protein. The cDNA derived of the human SQSTM1/p62 gene could be successfully inserted into the plasmid pET-28a(+), which made, after the transformation of E. coli cells, the expression of the SQSTM1/p62 protein and its purification by ?Immobilized Metal Affinity Chromatography? possible. The amount of purified soluble SQSTM1/p62 is sufficient for redox characterization of the protein. To be able to perform NMR studies, the efficiency of the protein purification has to be increased in order to obtain a higher yield of soluble SQSTM1/p62.