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Hormone-Sensitive Lipase (HSL)

Updated: 2026-07-17

Overview

Hormone-sensitive lipase (HSL) is an intracellular neutral lipase that catalyzes the hydrolysis of stored triglycerides in adipose tissue and other organs. It is a pivotal enzyme in lipid metabolism, releasing free fatty acids for energy production during fasting or exercise. HSL is highly regulated by hormones such as catecholamines (which activate it) and insulin (which inhibits it). Research on HSL has expanded due to its role in metabolic disorders like obesity and type 2 diabetes. Mouse HSL, in particular, is frequently used in preclinical studies to model human metabolic conditions. The enzyme's activity is measured in vitro using substrates like triolein or cholesterol esters.

Physical and Chemical Properties

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HSL is a serine esterase with a molecular weight of approximately 84-88 kDa, depending on the species and post-translational modifications. The enzyme exists in multiple isoforms due to alternative splicing. Its structure includes a regulatory N-terminal domain and a catalytic C-terminal domain. HSL operates optimally at physiological pH (7.0-7.5) and temperature (37°C). It requires phosphorylation at specific serine residues for full activation. The enzyme is typically supplied as a lyophilized powder or in buffered solutions for research use. Stability varies; some formulations include glycerol or albumin to prevent aggregation.

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Main Applications

HSL is primarily used in metabolic research to study lipolysis, adipose tissue function, and energy homeostasis. It serves as a biomarker in obesity and diabetes studies, where dysregulation of HSL activity is often observed. Pharmaceutical companies screen HSL inhibitors as potential anti-obesity or anti-diabetic drugs. In vitro, HSL is employed in enzymatic assays to quantify lipase activity or test modulator compounds. Recombinant mouse HSL is widely used to standardize assays due to its well-characterized kinetics. Additionally, HSL antibodies are utilized in immunohistochemistry to localize the enzyme in tissues.

Safety and Storage

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HSL is not classified as highly hazardous, but standard laboratory precautions apply. Use personal protective equipment (PPE) such as gloves and safety glasses when handling. Avoid inhalation of powders or aerosols. In case of skin contact, rinse thoroughly with water. For storage, lyophilized HSL should be kept at -20°C or -80°C in a desiccated environment. Reconstituted enzyme solutions are typically stable for weeks at 4°C or months at -80°C. Aliquotting is recommended to minimize freeze-thaw cycles, which can degrade activity. Always check the manufacturer's stability data for specific lots.

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B2B Procurement Guide

When procuring HSL for research or industrial use, prioritize suppliers with strict quality control (e.g., Sigma-Aldrich, Cayman Chemical, Abcam). Key specifications include purity (≥90% by SDS-PAGE), specific activity (e.g., μmol/min/mg protein), and absence of contaminating proteases. For bulk orders, request batch-specific certificates of analysis (CoA) detailing enzymatic activity, endotoxin levels, and stability. Consider recombinant vs. native HSL depending on application needs. Lead times vary; specialty isoforms (e.g., phosphorylated HSL) may require custom production. Pricing is often volume-dependent, with discounts available for long-term contracts.

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