p-APMSF (hydrochloride)
(Synonyms: (4-脒苯基)甲磺酰氟盐酸盐) 目录号 : GC40256
An irreversible inhibitor of serine proteases
Cas No.:74938-88-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
p-APMSF is an irreversible inhibitor of serine proteases with Ki values of 1.02, 1.18, 1.5, and 1.54 µM for bovine trypsin, human thrombin, bovine plasmin, and bovine Factor Xa, respectively. It is selective for these proteases over bovine chymotrypsin and acetylcholinesterase.
| Cas No. | 74938-88-8 | SDF | |
| 别名 | (4-脒苯基)甲磺酰氟盐酸盐 | ||
| Canonical SMILES | FS(CC1=CC=C(C(N)=N)C=C1)(=O)=O.Cl | ||
| 分子式 | C8H9FN2O2S • HCl | 分子量 | 252.7 |
| 溶解度 | DMSO: 50 mg/mL,Water: 25 mg/mL | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 3.9573 mL | 19.7863 mL | 39.5726 mL |
| 5 mM | 0.7915 mL | 3.9573 mL | 7.9145 mL |
| 10 mM | 0.3957 mL | 1.9786 mL | 3.9573 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
A novel low molecular weight hemorrhagic toxin from Trimeresurus flavoviridis (Vorojima) venom
J Nat Toxins 2002 Aug;11(3):155-63.PMID:12182535doi
A low molecular weight hemorrhagic toxin, LMHT, was isolated from the venom of Trimeresurus flavoviridis from Yorojima using Q-Sepharose column chromatography. The purified hemorrhagic toxin was homogeneous by disc polyacrylamide gel electrophoresis at pH 8.3, and Ouchterlony immunodiffusion. LMHT has a molecular weight of 16,500 and possesses hemorrhagic activity. It did not show casein, azocasein, azoalbumin, or TAME (tosyl-L-arginine methyl ester hydrochloride) hydrolytic activities. Hemorrhagic activity was inhibited by EDTA, TEP (tetraethylenepentamine), p-APMSF(p-amidinophenylmethanesulfonylfluoride HCl), and N-bromosuccinimide. The minimum hemorrhagic dose of this hemorrhagic toxin was 7.1 microg/mouse. LMHT induced hydrolysis of the Aa and Bbeta chains of bovine fibrinogen.
Purification and characterization of a thrombin like enzyme, elegaxobin II, with lys-bradykinin releasing activity from the venom of Trimeresurus elegans (Sakishima-Habu)
Toxicon 2003 Apr;41(5):559-68.PMID:12676434DOI:10.1016/s0041-0101(02)00363-x.
A thrombin like enzyme, named elegaxobin II, with Lys-bradykinin releasing activity was purified from the venom of Trimeresurus elegans (Sakishima-habu) by gel-filtration on Sephadex G-100, and ion-exchange chromatography on the Q-Sepharose Fast Flow. By this procedure, about 9mg of purified enzyme was obtained from 1.1g of the venom. The purified enzyme showed a single protein band, the molecular weight of which was estimated to be about 35,000Da by sodium dodecyl sulfate-PAGE) under reducing condition, and this enzyme was found to contain a carbohydrate moiety. The specific activity of this enzyme toward tosyl-L-arginine methyl ester (TAME) was 250 TAME units/mg of protein. This enzyme clotted only rabbit fibrinogen, whereas human and bovine fibrinogens were unaffected. In the fibrinogen-fibrin conversion, this enzyme released only fibrinopeptide A from rabbit fibrinogen, whereas it did not release fibrinopeptide B. Furthermore, elegaxobin II released Lys-bradykinin when the enzyme was incubated with bovine plasma. The esterase activity was inhibited by p-amidinophenylmethanesulfonyl fluoride hydrochloride (p-APMSF), suggesting that this enzyme is a serine protease. The N-terminal sequence (Val-Ile-Gly-Gly) of this enzyme was identical to the typical sequence of serine proteinases.
Characterization of Habu thrombin-like enzyme (THLE) with a new n-terminal sequence from the venom of Trimeresurus flavoviridis (Habu)
J Nat Toxins 2002 Aug;11(3):205-12.PMID:12182540doi
A thrombin-like enzyme with a new amino-terminal sequence was isolated from the venom of Trimeresurus flavoviridis using Q-Sepharose, CM-Cellulose, and HW55 column chromatographies. Homogeneity was confirmed by the formation of a single band in polyacrylamide gel electrophoresis. The enzyme has a molecular weight of 29,000 Da. This thrombin-like enzyme was inhibited by p-amidinophenylmethanesulfonyl fluoride hydrochloride (p-APMSF), and dithiothreitol (DTT) suggesting that serines and disulfide bonds are involved in the expression of the enzyme's clotting activity. This thrombin-like enzyme hydrolyzes the Aalpha-chain and Bbeta-chain of bovine fibrinogen. The enzyme was stable to heat treatment.
A new thrombin-like enzyme, flavoviridiobin from the venom of Trimeresurus flavoviridis (habu)
J Nat Toxins 2000 Nov;9(4):327-39.PMID:11126511doi
Fibrinopeptide A and B releasing enzyme, flavoviridiobin, was isolated from the venom of Trimeresurus flavoviridis using Q-Sepharose, CM-Cellulose, and Sephadex G-75 column chromatographies. Homogeneity was established by the formation of a single band in polyacrylamide gel electrophoresis, isoelectric focusing, and Ouchterlony immunodiffusion. The enzyme has a molecular weight of 48,000, isoelectric point of 8.1, consists of 237 total amino acid residues, and demonstrates clotting activity. However, no tosyl-L-arginine methyl ester (TAME) hydrolytic and kinin-releasing activities were observed. This clotting enzyme was inhibited by p-amidinophenylmethanesulfonyl fluoride hydrochloride (p-APMSF), benzamidine, and beta-mercaptoethanol, suggesting that serine, acidic amino acids, and disulfide bonds are involved in the expression of the enzyme's clotting activity. This thrombin-like enzyme hydrolyzes B beta-chain of human fibrinogen at first, followed by hydrolysis A alpha-chain. The enzyme was stable over the pH range of 7-10 and was shown to be heat resistant.
Thrombin-like enzyme, flavovilase, with kinin-releasing activity from Trimeresurus flavoviridis (habu) venom
J Nat Toxins 2001 Aug;10(3):239-48.PMID:11491463doi
A thrombin-like enzyme, flavovilase, with kinin-releasing activity was isolated, purified, and characterized from the venom of Trimeresurus flavoviridis (habu) using Sephadex G-100, DEAE-Cellulose, and CM-Cellulose column chromatographies. The final preparation was homogeneous as demonstrated by a single band on polyacrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and isoelectric focusing electrophoresis. The enzyme possesses a molecular weight of 26,500, an isoelectric point of 5.0, and consists of 247 total amino acid residues. Specific electrolytic activities of this enzyme on N-tosyl-L-arginine methyl ester (TAME) and N-benzoyl-L-arginine ethyl ester (BAEE) were determined to be 50.9 and 17.4 micromol/min/mg, respectively. The enzyme was inhibited by p-APMSF (p-amidinophenylmethanesulfonyl fluoride hydrochloride), beta-mercaptoethanol, and N-bromosuccinimide. Additionally, the enzyme was found stable to heat treatment. It was also observed that the enzyme cleaved a kininogen analog with the release of bradykinin.