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AB51487

Human Hormone sensitive lipase/HSL peptide

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Human Hormone sensitive lipase/HSL peptide is a Synthetic blocking peptide.

View Alternative Names

Hormone-sensitive lipase, HSL, Monoacylglycerol lipase LIPE, Retinyl ester hydrolase, REH, LIPE

Key facts

Tags

Tag free

Applications

BL

applications

Biologically active

No

Accession

Q05469

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 0.1% BSA

storage-buffer

Reactivity data

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

Product details

This product was previously labelled as Hormone sensitive lipase

Sequence info

[{"linker":null,"sequence":"","proteinLength":null,"predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Synthetic","expressionSystem":null,"accessionNumber":"Q05469","tags":[]}]

Properties and storage information

Form
Liquid
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C
False

General info

Function

Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (PubMed : 15716583, PubMed : 15955102, PubMed : 19800417, PubMed : 8812477). Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentially hydrolyzes the fatty acid (FA) esters at the sn-3 position of the glycerol backbone in DAGs (PubMed : 19800417). Preferentially hydrolyzes FA esters at the sn-1 and sn-2 positions of the glycerol backbone in TAGs (By similarity). Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production (By similarity).

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Post-translational modifications

Phosphorylation by AMPK reduces its translocation towards the lipid droplets.

Product protocols

Target data

Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (PubMed : 15716583, PubMed : 15955102, PubMed : 19800417, PubMed : 8812477). Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentially hydrolyzes the fatty acid (FA) esters at the sn-3 position of the glycerol backbone in DAGs (PubMed : 19800417). Preferentially hydrolyzes FA esters at the sn-1 and sn-2 positions of the glycerol backbone in TAGs (By similarity). Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production (By similarity).
See full target information LIPE

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