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|Reactivity||Human, Mouse, Rat|
|Calculated MW||24670 Da|
|Other Names||Acyl-protein thioesterase 1, APT-1, hAPT1, 312-, Lysophospholipase 1, Lysophospholipase I, LPL-I, LysoPLA I, LYPLA1, APT1, LPL1|
|Target/Specificity||A synthetic peptide corresponding to residues in human Acyl protein thioesterase 1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Function||Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity toward KCNMA1. Has low lysophospholipase activity.|
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Provided below are standard protocols that you may find useful for product applications.
Acyl-protein thioesterase 1 (APT1, Lysophospholipase 1) is a member of a family of critical enzymes, lysophospholipases, that act on biological membranes to regulate the multifunctional lysophospholipids (1). APT1 hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (2). The role of APT1 in regulating lysophospholipids is important because increased levels of lysophospholipids are detected in a variety of diseases, including atherosclerosis and hyperlipidemia (1). Regulated expression of acyl-protein thioesterase by PKC has been suggested to have important implications for signal transduction processes (3).
1. Wang A, et al. Biochim Biophys Acta. 1437(2):157-69, 1999 2. The UniProt Consortium, The Universal Protein Resource (UniProt). Nucleic Acids Res., 36:D190-D195 (2008) 3. Wang A, et al. Biochim Biophys Acta. 1484(2-3):207-14, 2000
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