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化驗
97%
mp
85-88 °C (lit.)
SMILES 字串
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 密鑰
ZDHCZVWCTKTBRY-UHFFFAOYSA-N
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應用
12-羟基十二烷酸用于合成具有可变单体比例的高分子量聚 [（12-羟基十二烷酸）-co-（12-羟基硬脂酸）] \ [聚 (12HD-co-12HS)] 样品，使用 12-羟基硬脂酸甲酯 。
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
其他客户在看
H A Dirven et al.
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
D E Jensen et al.
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.
P Jezek et al.
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+
D D Giera et al.
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
Elena Bailo et al.
Analytical and bioanalytical chemistry, 394(7), 1797-1801 (2009-06-16)
Surface-enhanced Raman scattering was used as a spectroscopic tool to investigate the changes brought upon cytochrome P450BSss after fatty acid binding. Differences in the spectra of substrate-free and substrate-bound enzyme were observed indicating the potential for this method to be
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