CLPP
CLPP (caseinolytic mitochondrial matrix peptidase proteolytic subunit) is the proteolytic component of the mitochondrial ClpXP complex. It is a serine peptidase of the S14 family that cleaves peptides and proteins in an ATP-dependent process within the mitochondrial matrix. Browse Assay Genie's current range of CLPP research reagents below, or read on for the biology behind the target.
CLPP is the protease component of the ClpXP complex, which cleaves peptides and various proteins in an ATP-dependent process. On its own the subunit has low peptidase activity, and its activity depends on the partner CLPX. The ClpXP complex can degrade the caseins CSN1S1, CSN2 and CSN3, as well as synthetic peptides in vitro. It may serve a fairly general, central housekeeping function rather than degrading specific substrates. In the mitochondrion, CLPP also cleaves PINK1.
The CLPP protein belongs to the peptidase S14 family and hydrolyses proteins into small peptides in the presence of ATP and magnesium. It is transported into the mitochondrial matrix and is associated with the inner mitochondrial membrane. The enzyme carries the EC number 3.4.21.92. The human CLPP gene is classified by HGNC within the AAA ATPases gene group, reflecting its close functional link to the ATPase partner of the ClpXP complex. The mouse ortholog is named Clpp.
The gene was previously described as the ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog of E. coli, a name that reflects its relationship to the bacterial Clp protease. Researchers studying mitochondrial proteostasis, PINK1 processing or ClpXP function often work with the CLPP protein, the CLPP gene or CLPP antibody and CLPP ELISA kit reagents to investigate expression and abundance.
CLPP acts as the proteolytic core of ClpXP, which may perform a general housekeeping role in degrading proteins within the mitochondrial matrix.
CLPP has low peptidase activity without CLPX, making it a key subject for studying how the ATPase and protease partners work together.
CLPP cleaves PINK1 in the mitochondrion, linking this protease to research on PINK1 handling inside the organelle.
ClpXP degrades caseins and synthetic peptides in vitro, providing a basis for investigating ATP-dependent proteolysis and substrate specificity.
CLPP is the protease subunit of the mitochondrial ClpXP complex. It cleaves peptides and proteins in an ATP-dependent process, and has low activity without CLPX. It may perform a general housekeeping function and cleaves PINK1 in the mitochondrion.
UniProt calls it ATP-dependent Clp protease proteolytic subunit, mitochondrial. Earlier HGNC names describe it as the ClpP caseinolytic protease, ATP-dependent, proteolytic subunit homolog (E. coli). No alternative gene symbols are recorded.
CLPP has a mouse ortholog, Clpp, and its earlier names refer to the E. coli ClpP homolog, indicating a link to the bacterial Clp protease. Check the datasheet of any product for its validated reactivity.
Partners and substrates of the ClpXP protease complex, including mitochondrial quality-control targets.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q16740; product specifications from Assay Genie datasheets.