Anti-PPAP2A (AB1) antibody produced in rabbit

Lipid phosphate phosphatases (LPP) dephosphorylate a variety of bioactive lipids including phosphatidate, lysophosphatidate, sphingosine 1-phosphate, and ceramide 1-phosphate.
The lipid phosphate phosphatase phosphatidic acid phosphatase type 2A/lipid phosphate phosphohydrolase type 1(PPAP2A, LLP1) dephosphorylates exogenous lysophosphatidate (LPA), a lipid mediator that stimulates cell proliferation and growth, and is involved in physiological and pathological processes such as wound healing, platelet activation, angiogenesis and the growth of tumours.

Anti-PPAP2A (AB1) polyclonal antibody reacts with human, zebrafish, mouse, rat, chicken, bovine, pig, and rabbit phosphatidic acid phosphatase type 2A proteins.

Synthetic peptide directed towards the middle region of human PPAP2A

Anti-PPAP2A (AB1) polyclonal antibody is used to tag phosphatidic acid phosphatase type 2A for detection and quantitation by Western blotting and in plasma by immunohistochemical (IHC) techniques. It is used as a probe to determine the roles of phosphatidic acid phosphatase type 2A as an integral membrane bioactive lipid phosphatase.

PPAP2A is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of PPAP2A is found to be regulated by androgen in a prostatic adenocarcinoma cell line.The protein encoded by this gene is a member of the phosphatidic acid phosphatase (PAP) family. PAPs convert phosphatidic acid to diacylglycerol, and function in de novo synthesis of glycerolipids as well as in receptor-activated signal transduction mediated by phospholipase D. This protein is an integral membrane glycoprotein, and has been shown to be a surface enzyme that plays an active role in the hydrolysis and uptake of lipids from extracellular space. The expression of this gene is found to be regulated by androgen in a prostatic adenocarcinoma cell line. At least two alternatively spliced transcript variants encoding distinct isoforms have been described.

Synthetic peptide located within the following region: DPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCMLFVAL

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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