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AB151829

Recombinant Human Lysophospholipase 1/LPL-I protein

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Recombinant Human Lysophospholipase 1/LPL-I protein is a Human Full Length protein, in the 1 to 230 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

대체 명칭 보기

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

주요 정보

Purity

>95% SDS-PAGE

ab151829 is greater than 95% pure, as determined by SEC-HPLC.

Endotoxin 레벨

< 1 EU/µg

발현 시스템

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Animal free

No

Carrier free

No

Species

Human

보관 버퍼

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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보완 제품

Reagents, Controls & Accessories

AB116029

Prestained Protein Ladder - Extra broad molecular weight (5 - 245 kDa)

SDS-PAGE - Prestained Protein Ladder - Extra broad molecular weight (5 - 245 kDa) (AB116029)

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  • 1
Proteins & Peptides

AB105129

Recombinant Human APT-2 protein (His tag N-Terminus)

SDS-PAGE - Recombinant Human APT-2 protein (His tag N-Terminus) (AB105129)

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  • 0
Primary Antibodies

AB91606

Anti-Lysophospholipase 1/LPL-I antibody [EPR3667]

20ul selling size|RabMAb|Recombinant|KO Validated

Western blot - Anti-Lysophospholipase 1/LPL-I antibody [EPR3667] (AB91606)

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Proteins & Peptides

AB113589

Recombinant Human MAFG protein (His tag N-Terminus)

SDS-PAGE - Recombinant Human MAFG protein (His tag N-Terminus) (AB113589)

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Proteins & Peptides

AB167886

Recombinant Human TUG protein (His tag N-Terminus)

SDS-PAGE - Recombinant Human TUG protein (His tag N-Terminus) (AB167886)

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  • 0
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Reactivity 정보

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

[{"linker":null,"sequence":"MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID","proteinLength":"Full Length","predictedMolecularWeight":"24.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":230,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O75608","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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특성 및 보관 정보

제형
Liquid
배송 시 보관 조건
Dry Ice
적절한 단기 보관 조건
-20°C
적절한 장기 보관 조건
-20°C
분주 정보
Upon delivery aliquot
보관 정보
Avoid freeze / thaw cycle
False
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추가 정보

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.
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일반 정보

기능

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).

서열 유사성

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

Subcellular localisation

Nucleus membrane

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제품 프로토콜

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타겟 정보

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
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Product promise

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