CLPP (caseinolytic mitochondrial matrix peptidase proteolytic subunit) protein contains an aqueous chamber formed by face-to-face assembly of the two heptameric rings that have proteolytic active sites within. It is a member of the peptidase family S14. The CLPP gene is localized to human chromosome 19p13.3.
Immunogen
CLPP (NP_006003, 178 a.a. ~ 277 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Monoclonal Anti-CLPP antibody produced in mouse has been used in Western Blotting.
Biochem/physiol Actions
CLPP (caseinolytic mitochondrial matrix peptidase proteolytic subunit) gene encodes a protease component of the Clp complex that hydrolyzes peptides and various proteins in the presence of ATP. The protein requires magnesium for its activity. CLPP is found to be associated with the inner mitochondrial membrane.
Physical form
Solution in phosphate buffered saline, pH 7.4
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Perrault syndrome is caused by recessive mutations in CLPP, encoding a mitochondrial ATP-dependent chambered protease
Emma M Jenkinson
American Journal of Human Genetics, 92 (2013)
Ablation of the mitochondrial complex IV assembly protein Surf1 leads to increased expression of the UPRMT and increased resistance to oxidative stress in primary cultures of fibroblasts
Mice deficient in the electron transport chain (ETC) complex IV assembly protein SURF1 have reduced assembly and activity of cytochrome c oxidase that is associated with an upregulation of components of the mitochondrial unfolded protein response (UPR(MT)) and increased mitochondrial
Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP
Caseinolytic peptidase P (ClpP) is a mammalian quality control protease that is proposed to play an important role in the initiation of the mitochondrial unfolded protein response (UPRmt), a retrograde signaling response that helps to maintain mitochondrial protein homeostasis. Mitochondrial
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