CLPP Antibody recognizes endogenous levels of total CLPP protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro263 of human CLPP protein. Antibodies are purified by protein A and peptide affinity chromatography.
原厂资料：
Specificity / Sensitivity
CLPP Antibody recognizes endogenous levels of total CLPP protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro263 of human CLPP protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The proteolytic component, Tetradecameric Peptidase (CLpP), is a hexamer in one of four ATP-dependent mitochondrial proteases (CLpXP). CLPP, one of the proteases, is an endopeptidase that is highly conserved among prokaryotes and eukaryotes, both at the level of amino acid sequence and quaternary structure. The active unit of CLPP is a barrel-shaped tetradecamer, Proteolysis of larger substrates is initiated by caseinolytic peptidase X (CLPX) which unfolds specific protein substrates. The unfolded polypeptide chain translocates into the CLPP proteolytic chamber for protein degradation within the interior chamber of mitochondria (1). Recessive mutations inCLPPcause Perrault Syndrome, a heterogeneous condition characterized by sensorineural hearing loss and ovarian failure (2).
Mutations in Parkin or PINK1 cause recessively inherited Parkinson’s disease. In healthy mitochondria, PINK1 is rapidly degraded by mitochondrial proteases and the proteasome. Upon mitochondrial depolarization, PINK1 accumulates on the mitochondrial surface, recruits Parkin from the cytosol, and initiates mitophagy. The mitochondrial proteases MPP, PARL, m-AAA and CLPP have been implicated in PINK1 degradation and cleavage (3).
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