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Protein kinase C (PKC) is a family of serine-threonine kinases, which are classified into three major groups: classical (?, ? and ?), novel (?, ?, ?, and ?) and atypical (?, ? and ?). PKC?1 consists of a C-terminal kinase domain and a N-terminal regulatory domain, formed by C1 domains (C1A and C1B) and a C2 domain. Activation of PKC ?1 involves recruitment to the membrane and interaction with phospholipids, Ca2+ and diacylglycerol. Furthermore, fully active protein results upon phosphorylation of the activation loop. PKC?1 is expressed in pancreatic islet cells, monocytes, brain, and many vascular tissues, including retina, kidney and heart and dysregulation is associated with pathogenic processes involved in diabetic microangiopathy such as ischaemia, leakage, neovascularisation and abnormal vasodilator function. The two isoforms, PKC?1 and PKC?2, are generated by alternative splicing from a single gene and differ at their C-terminus. Purified human recombinant protein kinase C beta 2 (PKC?2) containing amino acids 1-673 and having a molecular mass of 103.7 kDa. Protein features a GST tag. Purity > 90% (SDS PAGE).