Human PARL blocking peptide (CDBP2198)

Synthetic Human PARL blocking peptide for BL

Product Overview
Blocking peptide for anti-PARL antibody
Target
PARL
Nature
Synthetic
Species Reactivity
Human
Tag/Conjugate
Unconjugated
Application Notes
For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not suitable for human or animal consumption.
Procedure
None
Format
Liquid
Concentration
200 μg/ml
Size
50 μg
Buffer
PBS containing 0.02% sodium azide
Preservative
0.02% Sodium Azide
Storage
Store at -20℃, stable for one year.
UniProt ID
Antigen Description
This gene encodes a mitochondrial integral membrane protein. Following proteolytic processing of this protein, a small peptide (P-beta) is formed and translocated to the nucleus. This gene may be involved in signal transduction via regulated intramembrane proteolysis of membrane-tethered precursor proteins. Variation in this gene has been associated with increased risk for type 2 diabetes. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]
Function
peptidase activity; serine-type endopeptidase activity;
Synonyms
PARL; presenilin associated, rhomboid-like; PSARL; presenilins-associated rhomboid-like protein, mitochondrial; PRO2207; PSARL1; RHBDS1; rhomboid 7 homolog 1 (Drosophila); rhomboid 7 homolog 1; mitochondrial intramembrane cleaving protease PARL; mitochondrial intramembrane-cleaving protease PARL; PSENIP2;

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References


Rhomboid Protease PARL Mediates the Mitochondrial Membrane Potential Loss-induced Cleavage of PGAM5

JOURNAL OF BIOLOGICAL CHEMISTRY

Authors: Sekine, Shiori; Kanamaru, Yusuke; Koike, Masato; Nishihara, Ayako; Okada, Masahiro; Kinoshita, Hideyuki; Kamiyama, Miki; Maruyama, Junichi; Uchiyama, Yasuo; Ishihara, Naotada; Takeda, Kohsuke; Ichijo, Hidenori

Regulated intramembrane proteolysis is a widely conserved mechanism for controlling diverse biological processes. Considering that proteolysis is irreversible, it must be precisely regulated in a context-dependent manner. Here, we show that phosphoglycerate mutase 5 (PGAM5), a mitochondrial Ser/Thr protein phosphatase, is cleaved in its N-terminal transmembrane domain in response to mitochondrial membrane potential (Delta Psi(m)) loss. This Delta Psi(m) loss-dependent cleavage of PGAM5 was mediated by presenilin-associated rhomboid-like (PARL). PARL is a mitochondrial resident rhomboid serine protease and has recently been reported to mediate the cleavage of PINK1, a mitochondrial Ser/Thr protein kinase, in healthy mitochondria with intact Delta Psi(m). Intriguingly, we found that PARL dissociated from PINK1 and reciprocally associated with PGAM5 in response to Delta Psi(m) loss. These results suggest that PARL mediates differential cleavage of PINK1 and PGAM5 depending on the health status of mitochondria. Our data provide a prototypical example of stress-dependent regulation of PARL-mediated regulated intramembrane proteolysis.

Intramembrane Proteolysis of Mgm1 by the Mitochondrial Rhomboid Protease Is Highly Promiscuous Regarding the Sequence of the Cleaved Hydrophobic Segment

JOURNAL OF MOLECULAR BIOLOGY

Authors: Schaefer, Anja; Zick, Michael; Kief, Jan; Steger, Mirco; Heide, Heinrich; Duvezin-Caubet, Stephane; Neupert, Walter; Reichert, Andreas S.

Rhomboids are a family of intramembrane serine proteases that are conserved in bacteria, archaea, and eukaryotes. They are required for numerous fundamental cellular functions such as quorum sensing, cell signaling, and mitochondrial dynamics. Mitochondrial rhomboids form an evolutionarily distinct class of rhomboids. It is largely unclear how their activity is controlled and which substrate determinants are responsible for recognition and cleavage. We investigated these requirements for the mitochondrial rhomboid protease Pcp1 and its substrate Mgm1. In contrast to several other rhomboid proteases, Pcp1 does not require helix-breaking amino acids in the cleaved hydrophobic region of Mgm1, termed 'rhomboid cleavage region' (RCR). Even transmembrane segments of inner membrane proteins that are normally not processed by Pcp1 become cleavable when put in place of the authentic RCR of Mgm1. We further show that mutational alterations of a highly negatively charged region located C-terminally to the RCR led to a strong processing defect. Moreover, we show that the determinants required for Mgm1 processing by mitochondrial rhomboid protease are conserved during evolution, as PARL (the human ortholog of Pcp1) showed similar substrate requirements. These results suggest a surprising promiscuity of the mitochondrial rhomboid protease regarding the sequence requirements of the cleaved hydrophobic segment. We propose a working hypothesis on how the mitochondrial rhomboid protease can, despite this promiscuity, achieve a high specificity in recognizing Mgm1. This hypothesis relates to the exceptional biogenesis pathway of Mgm1. (C) 2010 Elsevier Ltd. All rights reserved.

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