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LYPLA1 Antibody (Center) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession O75608
Clone Names 110617022
Additional Information
Gene ID 10434
Other Names Acyl-protein thioesterase 1, APT-1, hAPT1, 312-, Lysophospholipase 1, Lysophospholipase I, LPL-I, LysoPLA I, LYPLA1, APT1, LPL1
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
Synonyms APT1, LPL1
Function Acts as a acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Has depalmitoylating activity toward KCNMA1 (PubMed:22399288). Could also depalmitoylate ADRB2 (PubMed:27481942). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (PubMed:19439193). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso- PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (PubMed:19439193). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (PubMed:21393252).
Cellular Location Cytoplasm. Cell membrane. Nucleus membrane. Endoplasmic reticulum. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum.
Tissue Location Platelets..
Research Areas
Citations (0)

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Lysophospholipases are enzymes that act on biologicalmembranes to regulate the multifunctional lysophospholipids. Theprotein encoded by this gene hydrolyzes lysophosphatidylcholine inboth monomeric and micellar forms. The use of alternatepolyadenylation sites has been found for this gene. There arealternatively spliced transcript variants described for this genebut the full length nature is not known yet.


Satou, M., et al. Endocrinology 151(10):4765-4775(2010)Dekker, F.J., et al. Nat. Chem. Biol. 6(6):449-456(2010)Hirano, T., et al. Biochim. Biophys. Acta 1791(8):797-805(2009)Siegel, G., et al. Nat. Cell Biol. 11(6):705-716(2009)Devedjiev, Y., et al. Structure 8(11):1137-1146(2000)

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$ 277.78
Cat# BP19062c
Availability: 2 weeks
Bulk Size

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