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Arphamenine B(hemisulfate)
本产品不向个人销售,仅用作科学研究,不用于任何人体实验及非科研性质的动物实验。
Arphamenine B(hemisulfate)图片
CAS NO:144110-38-3
包装与价格:
包装价格(元)
5mg电议
10mg电议

产品介绍

化学性质

Physical AppearanceA crystalline solid
StorageStore at -20°C
M.Wt385.4
Cas No.144110-38-3
FormulaC16H24N4O4·1/2H2SO4
Solubility≤0.2mg/ml in DMSO
Chemical NameαR-[(3S)-3-amino-6-[(aminoiminomethyl)amino]-2-oxohexyl]-4-hydroxy-benzenepropanoic acid, hemisulfate
Canonical SMILESO=C([C@@H](N)CCCNC(N)=N)C[C@H](C(O)=O)CC1=CC=C(O)C=C1.OS(O)(=O)=O
运输条件蓝冰运输或根据您的需求运输。
一般建议为了使其更好的溶解,请用37℃加热试管并在超声波水浴中震动片刻。不同厂家不同批次产品溶解度各有差异,仅做参考。若实验所需浓度过大至产品溶解极限,请添加助溶剂助溶或自行调整浓度。溶液形式一般不宜长期储存,请尽快用完。

资料参考

Arphamenine B is a specific inhibitor of aminopeptidase B first isolated from bacteria [1]. Aminopeptidase B (Ap-B) is a Zn2+-dependent exopeptidase which selectively removes Arg and/or Lys residues from the N terminus of several peptide substrates. Aminopeptidase B has been involved in processing events occurring either during its intracellular transport along the secretory pathway or at the plasma membrane level [2].

In vitro: Arphamenine B inhibited the activity of aminopeptidase enzyme with an IC50 value of 9.0 μM [2]. Arphamenine B strongly inhibited transport by the oligopeptide/H+ symporter with the EC50 values of 15 to 67 μM. Arphamenine at concentration 100 μM acted as either ineffective or weak inhibitor of membrane-associated hydrolysis [4]. Arphamenine selectively suppressed dipeptide hydrolysis [4].

References:
[1] Umezawa H, AOYAGI T, OHUCHI S, et al.  Arphamenines A and B, new inhibitors of aminopeptidase B, produced by bacteria[J]. The Journal of antibiotics, 1983, 36(11): 1572-1575.
[2] Balogh A, Cadel S, Foulon T, et al.  Aminopeptidase B: a processing enzyme secreted and associated with the plasma membrane of rat pheochromocytoma (PC12) cells[J]. Journal of Cell Science, 1998, 111(2): 161-169.
[3] Sajid M, Isaac R E, Harrow I D.  Purification and properties of a membrane aminopeptidase from Ascaris suum muscle that degrades neuropeptides AF1 and AF2[J]. Molecular and biochemical parasitology, 1997, 89(2): 225-234.
[4] Daniel H, Adibi S A.  Functional separation of dipeptide transport and hydrolysis in kidney brush border membrane vesicles[J]. The FASEB journal, 1994, 8(10): 753-759.