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PNPLA3 Antibody (N-term) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q9NST1
Clone Names 100324033
Additional Information
Gene ID 80339
Other Names Patatin-like phospholipase domain-containing protein 3, Acylglycerol O-acyltransferase, 231-, Adiponutrin, Calcium-independent phospholipase A2-epsilon, iPLA2-epsilon, PNPLA3, ADPN, C22orf20
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name PLPL3
Function Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA (PubMed:22560221). Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides (PubMed:15364929, PubMed:20034933, PubMed:22560221). In vitro may express hydrolytic activity against glycerolipids triacylglycerol, diacylglycerol and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety (PubMed:21878620). However, the triacylglycerol hydrolase activity is controversial and may be very low (PubMed:22560221). Possesses phospholipase A2 activity (PubMed:15364929).
Cellular Location Membrane; Single-pass type II membrane protein. Lipid droplet
Research Areas
Citations (0)
citation

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Background

The protein encoded by this gene is a triacylglycerollipase that mediates triacylglycerol hydrolysis in adipocytes. Theencoded protein, which appears to be membrane bound, may beinvolved in the balance of energy usage/storage in adipocytes.

References

Santoro, N., et al. Hepatology 52(4):1281-1290(2010)Valenti, L., et al. Hepatology 52(4):1274-1280(2010)Rotman, Y., et al. Hepatology 52(3):894-903(2010)Speliotes, E.K., et al. Hepatology 52(3):904-912(2010)Pare, G., et al. PLoS Genet. 6 (6), E1000981 (2010) :

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$ 277.78
Cat# BP16280a
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