| Identification | Back Directory | [Name]
ARM1 | [CAS]
68729-05-5 | [Synonyms]
ARM1
ARM-1
(ARM1)
4-(4-Benzylphenyl)-1,3-thiazol-2-amine
2-Thiazolamine, 4-[4-(phenylmethyl)phenyl]- | [Molecular Formula]
C16H14N2S | [MDL Number]
MFCD01816130 | [MOL File]
68729-05-5.mol | [Molecular Weight]
266.36 |
| Chemical Properties | Back Directory | [storage temp. ]
Store at -20°C | [solubility ]
≤1mg/ml in ethanol;10mg/ml in DMSO;15mg/ml in dimethyl formamide | [form ]
crystalline solid | [color ]
Off-white to light yellow |
| Hazard Information | Back Directory | [Description]
Leukotriene A4 (LTA4) hydrolase/aminopeptidase is a bifunctional zinc metalloenzyme that both catalyzes the synthesis of LTB4 from LTA4 and cleaves the chemotactic peptide Pro-Gly-Pro. ARM1 is a thiazolamine that inhibits LTB4 synthesis in human neutrophils (IC50 = ~0.5 μM) and conversion of LTA4 to LTB4 by purified LTA4 hydrolase (Ki = 2.3 μM). ARM1 does not significantly affect the hydrolysis of Pro-Gly-Pro by LTA4 hydrolase. | [Uses]
Leukotriene A4 (LTA4) hydrolase/aminopeptidase is a bifunctional zinc metalloenzyme that both catalyzes the synthesis of LTB4 from LTA4 and cleaves the chemotactic peptide Pro-Gly-Pro. ARM1 is a thiazolamine that inhibits LTB4 synthesis in human neutrophils (IC50 = ~0.5 μM) and conversion of LTA4 to LTB4 by purified LTA4 hydrolase (Ki = 2.3 μM). ARM1 does not significantly affect the hydrolysis of Pro-Gly-Pro by LTA4 hydrolase.[Cayman Chemical] | [storage]
Store at -20°C | [References]
[1]. stsiapanava a, olsson u, wan m, et al. binding of pro-gly-pro at the active site of leukotriene a4 hydrolase/aminopeptidase and development of an epoxide hydrolase selective inhibitor. proc natl acad sci u s a. 2014 mar 18;111(11):4227-32.
[2]. haeggstrm jz. leukotriene a4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene b4 biosynthesis. j biol chem. 2004 dec 3;279(49):50639-42.
[3]. snelgrove rj, jackson pl, hardison mt, et al. a critical role for lta4h in limiting chronic pulmonary neutrophilic inflammation. science. 2010 oct 1;330(6000):90-4. |
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