198781
12-Hydroxydodecanoic acid
97%
Synonym(s):
12-Hydroxylauric acid
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About This Item
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Assay
97%
mp
85-88 °C (lit.)
SMILES string
OCCCCCCCCCCCC(O)=O
InChI
1S/C12H24O3/c13-11-9-7-5-3-1-2-4-6-8-10-12(14)15/h13H,1-11H2,(H,14,15)
InChI key
ZDHCZVWCTKTBRY-UHFFFAOYSA-N
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Application
12-Hydroxydodecanoic acid was used in the synthesis of high molecular weight poly[(12-hydroxydodecanoate)-co-(12-hydroxystearate)] [poly(12HD-co-12HS)] samples with variable monomer ratios using methyl 12-hydroxystearate.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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FEBS letters, 408(2), 166-170 (1997-05-19)
Fatty acid (FA) uniport via mitochondrial uncoupling protein (UcP) was detected fluorometrically with PBFI, potassium-binding benzofuran phthalate and SPQ, 6-methoxy-N-(3-sulfopropyl)-quinolinium, indicating K+ and H+, respectively. The FA structural patterns required for FA flip-flop, UcP-mediated FA uniport, activation of UcP-mediated H+
Journal of chromatography, 564(1), 266-271 (1991-03-08)
The formation of omega-hydroxylauric acid from lauric acid is an indicator of the activity of cytochrome P-450 IV family proteins. The two main metabolites of lauric acid, (omega-1)-and omega-hydroxylauric acid, have been completely separated by reversed-phase high-performance liquid chromatography. Measurement
Fundamental and applied toxicology : official journal of the Society of Toxicology, 16(2), 348-355 (1991-02-01)
Assessment of hepatic omega-oxidation of fatty acids by cytochrome P450IV enzymes in toxicology studies can be a means of evaluating test compound effects on peroxisomal proliferation. Routine assay of omega-oxidation, however, requires a simpler method of enzymatic analysis than currently
The Biochemical journal, 331 ( Pt 2), 659-668 (1998-06-11)
An enzyme isolated from rat liver cytosol (native molecular mass 78. 3 kDa; polypeptide molecular mass 42.5 kDa) is capable of catalysing the NADH/NADPH-dependent degradation of S-nitrosoglutathione (GSNO). The activity utilizes 1 mol of coenzyme per mol of GSNO processed.
FEBS letters, 436(1), 67-70 (1998-10-15)
Human class I alcohol dehydrogenase was mutated at positions 57 and 115, exchanging for Asp and Arg respectively, in an attempt to introduce glutathione-dependent formaldehyde dehydrogenase characteristics. In addition, class III alcohol dehydrogenase, identical to glutathione-dependent formaldehyde dehydrogenase, was mutated
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