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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
36 kDa
species reactivity
mouse, rabbit, horse, pig, human, rat, dog
concentration
0.5 mg - 1 mg/mL
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... PARL(55486)
Immunogen
Synthetic peptide directed towards the N terminal region of human PARL
Application
Anti-PARL antibody produced in rabbit is suitable for western blotting at a concentration of 0.5μg/ml and for immunohistochemistry of paraffin-embedded tissue sections at a concentration of 4-8μg/ml.
Biochem/physiol Actions
Presenilin-associated rhomboid-like (PARL) is a mitochondrial rhomboid serine protease reported to mediate the cleavage of PINK1, a mitochondrial Ser/Thr protein kinase.
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Other Notes
Synthetic peptide located within the following region: SLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQ
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5.
Shiori Sekine et al.
The Journal of biological chemistry, 287(41), 34635-34645 (2012-08-24)
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
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