CLPP Antibody, HRP conjugated
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Product Specs
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Typically, we are able to ship your order within 1-3 business days of receipt. Delivery times may vary depending on the shipping method and location. Please consult your local distributor for specific delivery timeframes.
Synonyms
ATP dependent protease ClpAP (E coli) proteolytic subunit antibody; ATP dependent protease ClpAP proteolytic subunit antibody; ATP dependent protease ClpAP proteolytic subunit human antibody; ATP dependent proteolytic subunit homolog (E coli) antibody; ATP dependent proteolytic subunit homolog antibody; Caseinolytic peptidase ATP dependent proteolytic subunit homolog antibody; Caseinolytic protease ATP dependent proteolytic subunit E coli antibody; clpP antibody; ClpP caseinolytic peptidase ATP dependent proteolytic subunit antibody; ClpP caseinolytic peptidase ATP dependent proteolytic subunit homolog antibody; CLPP_HUMAN antibody; Endopeptidase Clp antibody; mitochondrial antibody; Putative ATP dependent Clp protease proteolytic subunit mitochondrial antibody; Putative ATP dependent Clp protease proteolytic subunit antibody; Putative ATP-dependent Clp protease proteolytic subunit antibody
Target Names
CLPP
Uniprot No.
Target Background
Function
The CLPP antibody, HRP conjugated, targets the protease component of the Clp complex. This protein plays a crucial role in the ATP-dependent cleavage of peptides and various proteins. While exhibiting low peptidase activity in the absence of CLPX, the Clp complex effectively degrades CSN1S1, CSN2, and CSN3, along with synthetic peptides (in vitro). This suggests a broad housekeeping function rather than specific substrate degradation. Notably, it cleaves PINK1 within the mitochondrion.
Gene References Into Functions
- Autophagy compensates for impaired energy metabolism in CLPXP-deficient Podospora anserina strains, extending their healthspan. PMID: 28449241
- Our research demonstrates that severe mitochondrial cardiomyopathy and diminished respiration due to DARS2 deficiency can be mitigated by the loss of CLPP, leading to increased de novo synthesis of individual OXPHOS subunits. PMID: 27154400
- We have identified eight families affected by Perrault syndrome. In five of these families, we found novel or previously reported variants in HSD17B4, LARS2, CLPP, and C10orf2. PMID: 26970254
- Our findings suggest that tumors utilize ClpXP-directed proteostasis to maintain mitochondrial bioenergetics, buffer oxidative stress, and enable metastatic competence. PMID: 27389535
- Data indicate that an endopeptidase Clp (ClpP) mutation was identified in two patients with Perrault syndrome type 3 within a Turkish family. PMID: 27087618
- ClpP proteases from E. coli, S. aureus, and human mitochondria exhibit preferences for specific amino acids in the P1, P2, and P3 positions. PMID: 26606371
- Utilizing optical trapping to analyze single-molecule ClpXP unfolding and translocation of substrates consisting of domains with varying stabilities and sequences, we discovered that ClpXP unfolds most domains through a single pathway, with kinetics dependent on the native fold and structural stability. PMID: 25083874
- Deletion of PaClpP results in an unexpected healthy phenotype and increased lifespan in the fungal aging model organism Podospora anserina. This phenotype can be reversed by expressing human ClpP. PMID: 23360988
- Perrault syndrome is caused by recessive mutations in CLPP. PMID: 23541340
- The N-terminal peptide of ClpP is a structural component of the substrate translocation channel and may also play a significant functional role. PMID: 15522782
- hClpX can regulate the appearance of hClpP peptidase activity in mitochondria and may influence the nature of degradation products released during ATP-dependent proteolytic cycles. PMID: 16115876
- We hypothesize that decreased levels of mitochondrial proteases Lon and ClpP may allow heat shock protein 60 substrate proteins to undergo more folding attempts. PMID: 18378094
Database Links
Involvement In Disease
Perrault syndrome 3 (PRLTS3)
Protein Families
Peptidase S14 family
Subcellular Location
Mitochondrion matrix.
Tissue Specificity
Detected in liver (at protein level). Predominantly expressed in skeletal muscle. Intermediate levels in heart, liver and pancreas. Low in brain, placenta, lung and kidney.
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