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HSL Antibody [M23F5]

Catalog No.: F1374

Application: Reactivity: Human, Mouse

Usage Information

Dilution
WB1:1000 IP1:100 IF1:200

Application
WB, IP, IF

Reactivity
Human, Mouse

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
81 kDa, 83 kDa

Datasheet & SDS

Biological Description

Specificity
HSL Antibody [M23F5] detects endogenous levels of total HSL protein.

Clone
M23F5

Synonym(s)
Hormone-sensitive lipase; HSL; Monoacylglycerol lipase LIPE; Retinyl ester hydrolase; REH; LIPE

Background
HSL (hormone-sensitive lipase) is an intracellular neutral lipase of the α/β-hydrolase superfamily, predominantly expressed in adipocytes, steroidogenic tissues, and skeletal muscle, where it acts as the rate-limiting enzyme for fatty acid mobilization from stored triacylglycerols during lipolysis. HSL displays the canonical α/β-hydrolase fold, with a central β-sheet of eight parallel strands flanked by 11 α-helices, organized into a catalytic domain (core hydrolase scaffold) and a regulatory cap domain. The active site triad consists of Ser188 (nucleophile in the GXSXG motif), His317 (proton shuttle), and Asp287 (stabilizer), buried about 25 Å from the surface in a deep, hydrophobic substrate-binding gorge lined by residues like Leu113, Tyr219, and Phe322, with acidic entrance residues such as Glu43 and Asp50 aiding substrate access. HSL hydrolyzes triacylglycerols, diacylglycerols, and cholesteryl esters, with its activity tightly controlled by reversible phosphorylation: PKA phosphorylates Ser563, Ser659, and Ser660 in response to cAMP-elevating hormones (e.g., catecholamines via β-adrenergic receptors), increasing catalytic activity, lipid droplet translocation, and hydrolysis; AMPK phosphorylation at Ser565 inhibits by blocking PKA sites, while MAPK acts at Ser600 to activate. Through these regulatory mechanisms, HSL integrates with energy homeostasis pathways, coupling lipolysis to adrenergic signaling and nutrient sensing. HSL deficiency results in impaired fat mobilization, obesity resistance, and metabolic disturbances, whereas dysregulation is implicated in dyslipidemia and type 2 diabetes.

Background

HSL (hormone-sensitive lipase) is an intracellular neutral lipase of the α/β-hydrolase superfamily, predominantly expressed in adipocytes, steroidogenic tissues, and skeletal muscle, where it acts as the rate-limiting enzyme for fatty acid mobilization from stored triacylglycerols during lipolysis. HSL displays the canonical α/β-hydrolase fold, with a central β-sheet of eight parallel strands flanked by 11 α-helices, organized into a catalytic domain (core hydrolase scaffold) and a regulatory cap domain. The active site triad consists of Ser188 (nucleophile in the GXSXG motif), His317 (proton shuttle), and Asp287 (stabilizer), buried about 25 Å from the surface in a deep, hydrophobic substrate-binding gorge lined by residues like Leu113, Tyr219, and Phe322, with acidic entrance residues such as Glu43 and Asp50 aiding substrate access. HSL hydrolyzes triacylglycerols, diacylglycerols, and cholesteryl esters, with its activity tightly controlled by reversible phosphorylation: PKA phosphorylates Ser563, Ser659, and Ser660 in response to cAMP-elevating hormones (e.g., catecholamines via β-adrenergic receptors), increasing catalytic activity, lipid droplet translocation, and hydrolysis; AMPK phosphorylation at Ser565 inhibits by blocking PKA sites, while MAPK acts at Ser600 to activate. Through these regulatory mechanisms, HSL integrates with energy homeostasis pathways, coupling lipolysis to adrenergic signaling and nutrient sensing. HSL deficiency results in impaired fat mobilization, obesity resistance, and metabolic disturbances, whereas dysregulation is implicated in dyslipidemia and type 2 diabetes.

References
https://pubmed.ncbi.nlm.nih.gov/14725507/ https://pubmed.ncbi.nlm.nih.gov/8029209/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%