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Phomopsinamine Sale

(Synonyms: Phomopsinamine A) 目录号 : GC48394

An inhibitor of microtubule polymerization

Phomopsinamine Chemical Structure

Cas No.:89085-54-1

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100µg
¥2,483.00
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500µg
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Sample solution is provided at 25 µL, 10mM.

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产品描述

Phomopsinamine is an inhibitor of microtubule polymerization and a derivative of phomopsin A .1 It inhibits the rate and extent of polymerization of tubulin isolated from ovine brain (IC50s = 0.53 and 0.59 µM, respectively).

1.Lacey, E., Edgar, J.A., and Culvenor, C.C.Interaction of phomopsin A and related compounds with purified sheep brain tubulinBiochem. Pharmacol.36(13)2133-2138(1987)

Chemical Properties

Cas No. 89085-54-1 SDF
别名 Phomopsinamine A
Canonical SMILES ClC1=CC([C@H](O)[C@@H]2NC)=CC(O[C@@](CC)(C)[C@@](NC([C@H](C(C)=C)NC2=O)=O)([H])C(N3[C@@](C(N/C(C(N)=O)=C(CC)\C)=O)([H])C=CC3)=O)=C1O
分子式 C32H43ClN6O8 分子量 675.2
溶解度 储存条件 -20°C
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1 mg 5 mg 10 mg
1 mM 1.481 mL 7.4052 mL 14.8104 mL
5 mM 0.2962 mL 1.481 mL 2.9621 mL
10 mM 0.1481 mL 0.7405 mL 1.481 mL
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Research Update

Interaction of phomopsin A and related compounds with purified sheep brain tubulin

Biochem Pharmacol 1987 Jul 1;36(13):2133-8.PMID:3606630DOI:10.1016/0006-2952(87)90141-9

Phomopsins comprise a family of peptide mycotoxins containing a 13-membered ring formed by an ether bridge, produced by the fungus Phomopsis leptostromiformis, the causal agent in lupin poisoning (lupinosis). The biochemical actions of two naturally occurring phomopsins, phomopsin A and B, and the chemical derivatives, Phomopsinamine A and octahydrophomopsin A, on purified sheep brain tubulin were investigated. All analogues were potent microtubule inhibitors, blocking the polymerization of tubulin at concentrations of less than 1 microM. They inhibited [3H]vinblastine binding to tubulin and, in common with vinblastine and its competitive inhibitor maytansine, enhanced the binding of [3H]colchicine to tubulin. It is postulated that phomopsin A and its analogues exert their action on tubulin by interaction at or near the vinblastine binding site. Two possible mechanisms for the interaction between vinblastine or phomopsins and colchicine binding to tubulin are proposed.