Phosphatidylserine Decarboxylase Proenzyme (PISD) Antibody

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Description
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.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | Phosphatidylserine Decarboxylase Proenzyme (PISD) |
Host | Rabbit |
Reactivity | Human, Mouse |
Recommended Dilution | WB: 1/500 - 1/2000. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Purified by affinity chromatography. |
Size 1 | 60 µl |
Size 2 | 120 µl |
Size 3 | 200 µl |
Form | Liquid |
Tested Applications | WB |
Buffer | PBS, pH 7.3, containing 0.01% thiomersal, 50% glycerol. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | Q9UG56 |
Gene ID | 23761 |
NCBI Accession | NP_055153.1 |
Background | Antibody anti-PISD |
Status | RUO |
Note | Concentration: 1 mg/ml - |
Descripción
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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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