With respect to acute toxicity, simple alcohols have low acute toxicities. Doses of several milliliters are tolerated. 24034-73-9, formula is C20H34O, For pentanols, hexanols, octanols and longer alcohols, LD50 range from 2–5 g/kg (rats, oral). Ethanol is less acutely toxic.All alcohols are mild skin irritants. Electric Literature of 24034-73-9
Kallemeijn, Wouter W.;Lanyon-Hogg, Thomas;Panyain, Nattawadee;Goya Grocin, Andrea;Ciepla, Paulina;Morales-Sanfrutos, Julia;Tate, Edward W. research published 《 Proteome-wide analysis of protein lipidation using chemical probes: in-gel fluorescence visualization, identification and quantification of N-myristoylation, N- and S-acylation, O-cholesterylation, S-farnesylation and S-geranylgeranylation》, the research content is summarized as follows. Protein lipidation is one of the most widespread post-translational modifications (PTMs) found in nature, regulating protein function, structure and subcellular localization. Lipid transferases and their substrate proteins are also attracting increasing interest as drug targets because of their dysregulation in many disease states. However, the inherent hydrophobicity and potential dynamic nature of lipid modifications makes them notoriously challenging to detect by many anal. methods. Chem. proteomics provides a powerful approach to identify and quantify these diverse protein modifications by combining bespoke chem. tools for lipidated protein enrichment with quant. mass spectrometry-based proteomics. Here, we report a robust and proteome-wide approach for the exploration of five major classes of protein lipidation in living cells, through the use of specific chem. probes for each lipid PTM. In-cell labeling of lipidated proteins is achieved by the metabolic incorporation of a lipid probe that mimics the specific natural lipid, concomitantly wielding an alkyne as a bio-orthogonal labeling tag. After incorporation, the chem. tagged proteins can be coupled to multifunctional capture reagents by using click chem., allowing in-gel fluorescence visualization or enrichment via affinity handles for quant. chem. proteomics based on label-free quantification (LFQ) or tandem mass-tag (TMT) approaches. In this protocol, we describe the application of lipid probes for N-myristoylation, N- and S-acylation, O-cholesterylation, S-farnesylation and S-geranylgeranylation in multiple cell lines to illustrate both the workflow and data obtained in these experiments We provide detailed workflows for method optimization, sample preparation for chem. proteomics and data processing. A properly trained researcher (e.g., technician, graduate student or postdoc) can complete all steps from optimizing metabolic labeling to data processing within 3 wk. This protocol enables sensitive and quant. anal. of lipidated proteins at a proteome-wide scale at native expression levels, which is critical to understanding the role of lipid PTMs in health and disease.
24034-73-9, Geranylgeraniol is a diterpenoid that is hexadeca-2,6,10,14-tetraene substituted by methyl groups at positions 3, 7, 11 and 15 and a hydroxy group at position 1. It has a role as a plant metabolite, a volatile oil component and an antileishmanial agent. It is a diterpenoid and a polyprenol.
Geranylgeraniol, a precursor to geranylgeranylpyrophosphate, is an intermediate in the mevalonate pathway. Geranylgeraniol has been shown to prevent bone re-absorption, inhibition of osteoclast formation, and kinase activation in vitro. When working with statins, Geranylgeraniol can reduce the toxicity without inhibiting the cholesterol-producing effects. Geranylgeraniol has been documented to counteract the effects of fluvastatin by inhibiting activation of caspase-1 and production of IL-1. Additionally Geranylgeraniol has been found to induce apoptosis in HL-60 cells.
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Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts