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AB168773

Anti-Lysophospholipase 1/LPL-I antibody

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(2 Publications )

Mouse Polyclonal Lysophospholipase 1/LPL-I antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human LYPLA1.

View Alternative Names

APT1, LPL1, LYPLA1, Acyl-protein thioesterase 1, APT-1, hAPT1, Lysophospholipase 1, Lysophospholipase I, Palmitoyl-protein hydrolase, LPL-I, LysoPLA I

Key facts

Host species

Mouse

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human LYPLA1.

O75608

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Lysophospholipase 1 also known as LPL-I is an enzyme involved in lipid metabolism. It catalyzes the hydrolysis of lysophospholipids into fatty acids and glycerophospholipids. The molecular mass of Lysophospholipase 1 is approximately 25 kDa. This protein is expressed in various tissues including heart liver and brain. Alternate names for this enzyme include APEH and acylaminoacyl-peptidase reflecting its ability to hydrolyze peptides and acyl groups.
Biological function summary

Lysophospholipase 1 plays a role in maintaining lipid homeostasis. It does not function as part of a larger protein complex acting independently in the regulation of lipid turnover. By breaking down lysophospholipids the enzyme helps balance the cellular lipid composition ensuring proper membrane integrity and cellular signaling. This regulation is critical in tissues that have high turnover of lipids like the brain and liver.

Pathways

Lysophospholipase 1 participates in lipid metabolism and glycerophospholipid biosynthesis pathways. The enzyme helps process intermediates in these pathways facilitating energy production and phospholipid remodeling. In terms of related proteins LPL-I functions in coordination with phospholipase A2 in lipid degradation and this relationship impacts the synthesis of bioactive lipid mediators.

Lysophospholipase 1 has been linked to metabolic disorders and neurological diseases. Altered activity of this enzyme has correlations with conditions such as metabolic syndrome where lipid imbalances occur. Moreover its dysregulation can influence neurological disorders like Alzheimer's Disease due to its impact on lipid signaling. In these contexts LPL-I interacts functionally with other enzymes like phospholipase A2 which also plays a role in lipid signaling and homeostasis.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Acts as an 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). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (PubMed : 22399288, PubMed : 27481942, PubMed : 37802024). Acts as a negative regulator of autophagy by mediating palmitoylation of SQSTM1, decreasing affinity between SQSTM1 and ATG8 proteins and recruitment of ubiquitinated cargo proteins to autophagosomes (PubMed : 37802024). 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).
See full target information LYPLA1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Cell death discovery 11:166 PubMed40216750

2025

MGP regulates the adipogenic differentiation of mesenchymal stem cells in osteoporosis via the Ca2+/CaMKII/RIP140/FABP3 axis.

Applications

Unspecified application

Species

Unspecified reactive species

Xinglang Wang,Yunhui Zhang,Chenhao Xu,Quanfeng Li,Pengfei Ji,Huatao Liu,Yibin Zhang,Jiahao Jin,Zihao Yuan,Miao Yuan,Pei Feng,Yanfeng Wu,Wenjie Liu,Huiyong Shen,Peng Wang

PloS one 11:e0153256 PubMed27058953

2016

Temporal Analysis of Gene Expression in the Murine Schwann Cell Lineage and the Acutely Injured Postnatal Nerve.

Applications

Unspecified application

Species

Unspecified reactive species

Anjali Balakrishnan,Morgan G Stykel,Yacine Touahri,Jo Anne Stratton,Jeff Biernaskie,Carol Schuurmans
View all publications

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