CAS NO: | 144110-38-3 |
包装 | 价格(元) |
5mg | 电议 |
10mg | 电议 |
Physical Appearance | A crystalline solid |
Storage | Store at -20°C |
M.Wt | 385.4 |
Cas No. | 144110-38-3 |
Formula | C16H24N4O4·1/2H2SO4 |
Solubility | ≤0.2mg/ml in DMSO |
Chemical Name | αR-[(3S)-3-amino-6-[(aminoiminomethyl)amino]-2-oxohexyl]-4-hydroxy-benzenepropanoic acid, hemisulfate |
Canonical SMILES | O=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。 |
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.