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AB101156

Recombinant Mouse Lysophospholipase 1/LPL-I protein

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Recombinant Mouse Lysophospholipase 1/LPL-I protein is a Mouse Full Length protein, in the 1 to 230 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Apt1, Pla1a, Lypla1, Acyl-protein thioesterase 1, APT-1, Lysophospholipase 1, Lysophospholipase I, Palmitoyl-protein hydrolase, LPL-I, LysoPLA I

1 Images
SDS-PAGE - Recombinant Mouse Lysophospholipase 1/LPL-I protein (AB101156)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Mouse Lysophospholipase 1/LPL-I protein (AB101156)

15% SDS-PAGE showing ab101156 at approximately 26.8 kDa (3 μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

P97823

Animal free

No

Carrier free

No

Species

Mouse

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSPHIKYICPHAPVMPVTLNMNMAMPSWFDIVGLSPDSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSANRDISVLQCHGDCDPLVPLMFGSLTVERLKALINPANVTFKIYEGMMHSSCQQEMMDVKHFIDKLLPPID","proteinLength":"Full Length","predictedMolecularWeight":"26.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":230,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P97823","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

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.

Specifications

Form

Liquid

Additional notes

ab101156 is purified using conventional chromatography techniques.

General info

Function

Acts as an acyl-protein thioesterase (By similarity). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (By similarity). 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 (By similarity). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (By similarity). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS) (PubMed : 9139730). Has much higher thioesterase activity than lysophospholipase activity (By similarity). 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 (By similarity).

Sequence similarities

Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.

Subcellular localisation

Nucleus membrane

Product protocols

Target data

Acts as an acyl-protein thioesterase (By similarity). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (By similarity). 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 (By similarity). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (By similarity). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS) (PubMed : 9139730). Has much higher thioesterase activity than lysophospholipase activity (By similarity). 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 (By similarity).
See full target information Lypla1

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