110349-82-1

Basic information

• Product Name: 2-(1-hydroxypentyl)phenol
• Synonyms: 2-(1-hydroxypentyl)phenol
• CAS NO: 110349-82-1
• Molecular Weight: 180.247
• Mol File: 110349-82-1.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: 2-(1-hydroxypentyl)phenol(CAS DataBase Reference)
• NIST Chemistry Reference: 2-(1-hydroxypentyl)phenol(110349-82-1)
• EPA Substance Registry System: 2-(1-hydroxypentyl)phenol(110349-82-1)

Safety Data

• Hazardous Substances Data: 110349-82-1(Hazardous Substances Data)

Upstream product

• 693-03-8 n-butyl magnesium bromide 
• 90-02-8 salicylaldehyde 
• 109-65-9 1-bromo-butane 
• 89-95-2 2-methyl-benzyl alcohol 
• 693-04-9 butyl magnesium bromide 
• 122-56-5 tributyl borane 
• 583-03-9 1-Phenyl-1-pentanol 

Downstream Products

• 18430-91-6 1-(2-hydroxyphenyl)pentan-1-one 
• 1422447-37-7 2-(1-p-tosylpentyl)phenol 

Relevant articles and documents

One-Pot Ortho Hydroxylation of 2-(1-Hydroxyalkyl)naphthalenes and (1-Hydroxyalkyl)benzenes

Hydroxylations of 2-(1-hydroxyalkyl)-1,4,5,8(or 1,4,5,6,8)-tetra(or penta)methoxynaphthalenes and 2-(1-hydroxyalkyl)-1,4-dimethoxybenzenes at the 3-position were accomplished by a one-spot procedure.The same procedure has been found to be applicable to 2-(1-hydroxyalkyl)naphthalenes and (1-hydroxyalkyl)benzenes having no methoxy substituent.

Organocatalytic Phosphonylation of in Situ Formed o-Quinone Methides

A new class of Br?nsted acid catalysts based on N-heterocyclic phosphorodiamidic acids (NHPAs) has been developed. The NHPA catalyst promotes phospha-Michael addition reaction of trialkylphosphites to in situ generated ortho-quinone methides (o-QMs) for t

Targeting the gatekeeper residue in phosphoinositide 3-kinases

A single residue in the ATP binding pocket of protein kinases-termed the gatekeeper-has been shown to control sensitivity to a wide range of small molecule inhibitors (Chem. Biol. 2004, 11, 691; Chem. Biol. 1999, 6, 671). Kinases that possess a small side chain at this position (Thr, Ala, or Gly) are readily targeted by structurally diverse classes of inhibitors, whereas kinases that possess a larger residue at this position are broadly resistant. Recently, lipid kinases of the phosphoinositide 3-kinase (PI3-K) family have become the focus of intense research interest as potential drug targets (Chem. Biol. 2003, 10, 207; Curr. Opin. Pharmacol. 2003, 3, 426). In this study, we identify the residue that corresponds structurally to the gatekeeper in PI3-Ks, and explore its importance in controlling enzyme activity and small molecule sensitivity. Isoleucine 848 of p110α was mutated to alanine and glycine, but the mutated kinase was found to have severely impaired enzymatic activity. A structural bioinformatic comparison of this kinase with its yeast orthologs identified second site mutations that rescued the enzymatic activity of the I848A kinase. To probe the dimensions of the gatekeeper pocket, a focused panel of analogs of the PI3-K inhibitor LY294002 was synthesized and its activity against gatekeeper mutated and wild-type p110α was assessed.