PISD antibody

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935106861
info@markelab.com
name
PISD antibody
category
Primary Antibodies
provider
FineTest
reference
FNab06469
tested applications
ELISA, WB, IHC, IP

Description

Catalyzes the formation of phosphatidylethanolamine(PtdEtn) from phosphatidylserine(PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.

Documents del producto

Instrucciones
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Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
phosphatidylserine decarboxylase (PISD)
Host
Rabbit
Reactivity
Human, Mouse, Rat
Recommended Dilution
WB: 1:500-1:2000; IP: 1:200-1:1000; IHC: 1:20-1:200
Clonality
polyclonal
Conjugation
Unconjugated
Isotype
IgG
Observed MW
50~55 kDa
Purity
≥95% as determined by SDS-PAGE
Purification
Immunogen affinity purified
Size 1
100µg
Form
liquid
Tested Applications
ELISA, WB, IHC, IP
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
UniProt ID
Q9UG56
Gene ID
23761
Alias
Phosphatidylserine decarboxylase proenzyme, mitochondrial,Phosphatidylserine decarboxylase beta chain,Phosphatidylserine decarboxylase alpha chain,PISD
Background
Antibody anti-PISD
Status
RUO
Note
Mol. Weight 50~55 kDa

Descripción

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PISD antibody

Catalyzes the formation of phosphatidylethanolamine(PtdEtn) from phosphatidylserine(PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.

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Phosphatidylserine Decarboxylase Proenzyme (PISD) Antibody

PISD Antibody is a Rabbit Polyclonal antibody against PISD. Phosphatidylserine decarboxylases (PSDs; EC 4.1.1.65) catalyze the formation of phosphatidylethanolamine (PE) by decarboxylation of phosphatidylserine (PS). Type I PSDs, such as PISD, are targeted to the inner mitochondrial membrane by an N-terminal targeting sequence. PISD also contains a conserved LGST motif that functions as an autocatalytic cleavage site where the proenzyme is split into mature alpha and beta subunits (Schuiki and Daum, 2009.

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