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product name
弗林蛋白酶抑制剂 II,
化驗
≥95% (HPLC)
形狀
lyophilized
成份
Peptide Content, ≥48%
儲存條件
protect from light
技術
protein extraction: suitable
儲存溫度
−20°C
Amino Acid Sequence
Mpa-Mpa-Mpa-Mpa-Mpa-Mpa
一般說明
弗林蛋白酶是一种钙依赖性丝氨酸内蛋白酶，属于枯草杆菌蛋白酶样前蛋白/激素转换酶（PC）家族。它分布广泛，并且可在反式高尔基网络、细胞表面和内体之间有节规律的移动。
應用
弗林蛋白酶抑制剂II已作为弗林蛋白酶抑制剂用于：
- 研究在非致瘤性永生化人类颗粒细胞系（SVOG）中，其对转化生长因子β1（TGF-β1） 诱导的神经胶质细胞系衍生的神经营养因子（GDNF）产生的影响。
- 研究其对人肾2（HK-2）细胞中牛血清白蛋白（BSA）诱导的肾素（原）受体（PRR）裂解的作用。
- 用于弗林蛋白酶裂解试验中。
生化／生理作用
弗林蛋白酶在几种前蛋白的加工中起作用，例如骨形态发生蛋白4（BMP-4）、胰岛素受体和Notch1受体。它还可以处理人类免疫缺陷病毒1（HIV-1）糖蛋白gp160、几种金属蛋白酶、以及β-神经增长因子前体（β-NGF前体）。弗林蛋白酶还可参与转化生长因子 β1（TGF-β1）的裂解。
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
其他客户在看
A Cameron et al.
The Journal of biological chemistry, 275(47), 36741-36749 (2000-08-26)
The ubiquitous serine endoprotease furin has been implicated in the activation of bacterial toxins and viral glycoproteins as well as in the metastatic progression of certain tumors. Although high molecular mass bioengineered serpin inhibitors have been well characterized, no small
Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme
Dubois C M, et al.
The American Journal of Pathology, 158(1), 305-316 (2001)
Marcel Westenberg et al.
Journal of virology, 76(1), 178-184 (2001-12-12)
The Spodoptera exigua multicapsid nucleopolyhedrovirus (SeMNPV) Se8 gene was recently shown to encode the viral envelope fusion (F) protein. A 60-kDa C-terminal subunit (F1) of the 76-kDa primary translation product of this gene was found to be the major envelope
Miroslav S Sarac et al.
Infection and immunity, 72(1), 602-605 (2003-12-23)
The anthrax toxin protective antigen precursor is activated by proteolytic cleavage by furin or a furin-like protease. We present here data demonstrating that the small stable furin inhibitor hexa-D-arginine amide delays anthrax toxin-induced toxemia both in cells and in live
Miroslav S Sarac et al.
Infection and immunity, 70(12), 7136-7139 (2002-11-20)
The Pseudomonas aeruginosa exotoxin A (PEA) protein requires furin-mediated cleavage for manifestation of toxicity. We show here that the small stable furin inhibitor hexa-D-arginine amide effectively blocks PEA-induced cell lysis and is itself noncytotoxic. Administration of hexa-D-arginine to PEA-treated mice
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