Description
Full-length recombinant human SIRT4 was expressed in E. coli cells using an N-terminal GST tag.
Scientific Background: SIRT4 is a member of the sirtuin family of proteins which are homologs to the yeast Sir2 protein. Sirtuin family contain a sirtuin core domain and are grouped into four classes with SIRT4 being a member of class IV. SIRT4 lacks deacetylase activity but has ADP-ribosyltransferase activity (1). Immunoprecipitation analysis shows that SIRT4 interacts with the mitochondrial enzyme glutamate dehydrogenase (GDH), and functional analysis show that SIRT4 ADP-ribosylates and inhibits GDH (2). Downregulation of SIRT4 by RNA interference activates GDH, thereby upregulating insulin secretion in response to glucose and amino acids