A phospho-specific peptide corresponding to residues surrounding Serine 855 of human HSL was used as an immunogen. The antibody only detects HSL phosphorylated on Serine 855.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Hormone-sensitive lipase (HSL) is a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis. It is acutely controlled through reversible phosphorylation by catecholamines and insulin (1). HSL is the rate-limiting enzyme in hydrolysis of triglycerides in adipose tissue and of cholesteryl esters in steroidogenic tissues including the adrenals, ovaries, testes, and macrophages (2, 3). HSL activity has been positively correlated with free and esterified cholesterol ratios in seminiferous tubules (STf) and interstitial tissue (ITf) enriched fractions, but not with triglyceride levels, during testicular development. HSL is localized to elongated spermatids and Sertoli cells, where its distribution is stage-dependent, and within the cells lining the excurrent ducts of the testis. The HSL protein levels and enzymatic activity in ITf and STf were reported positively correlated with serum testosterone levels during development (4).
Related Pathway
Adipogenesis
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Western blot analysis on Human skeletal muscle lysates using anti-Phospho-HSL (pS855), 1:5000 dilution. Cells were either (A) untreated (B) treated with LP
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