CLPP Human
Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.
Description
CLPP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (57-277 a.a.) and having a molecular mass of 24.2kDa.
CLPP is purified by proprietary chromatographic techniques.
Product Specs
Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.
MPLIPIVVEQ TGRGERAYDI YSRLLRERIV CVMGPIDDSV ASLVIAQLLF LQSESNKKPI HMYINSPGGV VTAGLAIYDT MQYILNPICT WCVGQAASMG SLLLAAGTPG MRHSLPNSRI MIHQPSGGAR GQATDIAIQA EEIMKLKKQL YNIYAKHTKQ SLQVIESAME RDRYMSPMEA QEFGILDKVL VHPPQDGEDE PTLVQKEPVE AAPAAEPVPA ST.
Product Science Overview
The ClpP protease was first identified in Escherichia coli as part of the ClpAP complex, which consists of a regulatory unit (ClpA) with chaperone characteristics and an ATPase domain, and a proteolytic subunit (ClpP) . The human homolog of ClpP was later identified through sequence homology and was found to be encoded by the CLPP gene located on chromosome 19 .
ClpP is a barrel-shaped protease that forms a heptameric ring structure. In humans, ClpP can interact with ClpX, another ATPase, to form the ClpXP complex. This complex consists of two heptameric rings of ClpP flanked by hexameric rings of ClpX on either side . The interaction with ClpX is crucial for the proteolytic activity of ClpP, as it enhances the enzyme’s ability to degrade protein substrates .
ClpP is involved in the degradation of abnormal or misfolded proteins within the mitochondria, a process essential for maintaining cellular homeostasis. The enzyme cleaves peptides in various proteins, a process that requires ATP hydrolysis . This proteolytic activity is part of the mitochondrial unfolded-protein response, a stress signaling pathway that helps the cell manage protein quality under stress conditions .
Recombinant human ClpP is produced using genetic engineering techniques, where the CLPP gene is cloned and expressed in a suitable host, such as E. coli. This allows for the production of large quantities of the enzyme for research and therapeutic purposes . Recombinant ClpP retains the structural and functional properties of the native enzyme, making it a valuable tool for studying mitochondrial proteostasis and related diseases.
Mutations in the CLPP gene have been associated with Perrault syndrome, a rare genetic disorder characterized by sensorineural hearing loss and ovarian dysgenesis . Understanding the function and regulation of ClpP can provide insights into the pathogenesis of such disorders and potentially lead to the development of targeted therapies.
