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Aprotinin, serine protease inhibitor
NMR and HPLC COA下载 MSDS下载 - Names：
Aprotinin
- CAS号：
9087-70-1
MDL Number： MFCD00162935 - MF(分子式)： C284H432N84O79S7 MW(分子量)： 6511.44
- EINECS:232-994-9 Reaxys Number:
- Pubchem ID: Brand:BIOFOUNT
抑肽酶(9087-70-1,Aprotinin)是通过三个二硫键交联的单链多肽（58个氨基酸），显示出竞争性和可逆性抑制蛋白水解和酯水解活性。 抑肽酶形成稳定的复合物并阻断丝氨酸蛋白酶的活性位点。 大多数抑肽酶-蛋白酶复合物在pH> 10或<3（最适pH 5-7）下解离，结合是可逆的。 有效浓度与蛋白酶等摩尔。 抑肽酶在多肽激素的放射免疫测定中用作蛋白水解抑制剂。
| 货品编码 | 规格 | 纯度 | 价格 (¥) | 现价(¥) | 特价(¥) | 库存描述 | 数量 | 总计 (¥) |
|---|---|---|---|---|---|---|---|---|
| SS2583-5mg | 5mg | 来源于牛肺，冻干粉, 3-8 TIU | ¥ 112.00 | ¥ 112.00 | Instock1-2days | ¥ 0.00 |
| 中文别名 | Aprotinin, 丝氨酸蛋白酶抑制剂;抑肽酶(9087-70-1,Aprotinin);重组抑肽酶;抑肽酶(来源于牛肺,胰蛋白酶抑制剂);蛋白酶抑制剂(抑肽酶);重组胰蛋白酶抑制剂;抗蛋白酶肽(牛肺);抑肽酶(牛肺) |
| 英文别名 | Aprotinin, serine protease inhibitor;Aprotinin(9087-70-1);Aprotinin from bovine lung;Antilysin;Antikrein |
| CAS号 | 9087-70-1 |
| Inchi | InChI=1S/C20H26N2O2.BrH/c1-3-13-12-22-9-7-14(13)10-19(22)20(23)16-6-8-21-18-5-4-15(24-2)11-17(16)18;/h4-6,8,11,13-14,19-20,23H,3,7,9-10,12H2,1-2H3;1H/t13-,14?,19-,20+;/m0./s1 |
| InchiKey | BKKQYYLUFOIOJF-YYQSSQEESA-N |
| 分子式 Molecular Weight | C284H432N84O79S7 |
| 分子量 Formula | 6511.44 |
| 溶解度Solubility | H2O : 100 mg/mL (15.36 mM; Need ultrasonic) |
| 性状 | 白色至灰白色固体粉末 |
| 储藏条件 Storage conditions | 储存温度2-8℃ |
抑肽酶(9087-70-1,Aprotinin)实验注意事项：
1.实验前需戴好防护眼镜，穿戴防护服和口罩，佩戴手套，避免与皮肤接触。
2.实验过程中如遇到有毒或者刺激性物质及有害物质产生，必要时实验操作需要手套箱内完成以免对实验人员造成伤害。
3.取样品的移液枪头需及时更换，必要时为避免交叉污染尽可能选择滤芯吸头。
4.称量药品时选用称量纸，并无风处取药和称量以免扬撒，试剂的容器使用前务必确保干净，并消毒。
5.取药品时尽量采用多个药勺分别使用，使用后清洗干净后，烘干消毒存放。
6.实验后产生的废弃物需分类存储，并交于专业生物废气物处理公司处理，以免造成环境污染。
Aprotinin(9087-70-1) Experimental considerations:
1. Wear protective glasses, protective clothing and masks, gloves, and avoid contact with the skin during the experiment.
2. The waste generated after the experiment needs to be stored separately, and handed over to a professional biological waste gas treatment company to avoid environmental pollution.
Tag:抑肽酶(9087-70-1,Aprotinin),抑肽酶的作用,抑肽酶的活性,抑肽酶的纯度,抑肽酶的价格,抑肽酶的生产厂家,抑肽酶的注意事项,抑肽酶合成路线,抑肽酶的价格,抑肽酶的储存条件,抑肽酶的外观,抑肽酶的活性成分
| 产品说明 | 抑肽酶(9087-70-1,Aprotinin)仅做科学研究以及化学合成中间体使用,9087-70-1的活性、9087-70-1的MSDS等参数见主页 |
| Introduction | Aprotinin (9087-70-1, 抑肽酶) is only used for scientific research and chemical synthesis intermediates. The activity of 9087-70-1 and the MSDS of 9087-70-1 are available on the homepage |
| Application1 | 抑肽酶是小蛋白牛胰胰蛋白酶抑制剂 |
| Application2 | 抑肽酶是一种抗纤溶蛋白的分子，可抑制胰蛋白酶和相关的蛋白水解酶。 |
| Application3 | 抑肽酶还用作蛋白质纯化工具，以防止组织样品中存在的蛋白酶降解目标蛋白质。 |
Aprotinin is the small protein bovine pancreatic trypsin inhibitor (BPTI). It is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. It is a competitive serine protease inhibitor which blocks the active sites of enzyme by forming stable complexes with. It is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges. It is used as medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. It is used clinically to prevent postoperative blood loss and reduce transfusion requirements in those procedures which employ extracorporeal circulation. It is also used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest. It was temporarily withdrawn worldwide in 2007. It was reverted its previous standpoint regarding aprotinin by the European Medicines Agency (EMA) scientific committeeand in February 2012.
| 警示图 | |
| 危险性 | warning |
| 危险性警示 | No data available |
| 安全声明 | H317,H334 |
| 安全防护 | P261,P280,P342+P311 |
| 备注 | 实验过程中防止吸入、食入，做好安全防护 |
| 象形图 |   |
|---|---|
| 信号 | Danger |
| GHS危险说明 |
H302 (25%): Harmful if swallowed [Warning Acute toxicity, oral] H317 (75%): May cause an allergic skin reaction [Warning Sensitization, Skin] H334 (75%): May cause allergy or asthma symptoms or breathing difficulties if inhaled [Danger Sensitization, respiratory] |
| 防范说明代码 |
P261, P264, P270, P272, P280, P285, P301+P312, P302+P352, P304+P341, P321, P330, P333+P313, P342+P311, P363, and P501 (The corresponding statement to each P-code can be found at the GHS Classification page.) |
| 1.A new anti-fibrinolytic hemostatic compound 8-O-acetyl shanzhiside methylester extracted from Lamiophlomis rotata. |
| 2.Biological and Enzymatic Characterization of Proteases from Crude Venom of the Ant Odontomachus bauri. |
| 3.(99m) Tc-aprotinin - optimisation and validation of radiolabelling kits for routine preparation for diagnostic imaging of amyloidosis. |
| 4.Contribution of the Kallikrein/Kinin System to the Mediation of ConA-Induced Inflammatory Ascites. |
| The serine protease inhibitor camostat inhibits influenza virus replication and cytokine production in primary cultures of human tracheal epithelial cells |
1.A new anti-fibrinolytic hemostatic compound 8-O-acetyl shanzhiside methylester extracted from Lamiophlomis rotata.
Fan PC1, Ma HP1, Hao Y2, He XR2, Sun AJ1, Jiang W2, Li MX1, Jing LL1, He L2, Ma J3, Jia ZP4. J Ethnopharmacol. 2016 Apr 13. pii: S0378-8741(16)30206-9. doi: 10.1016/j.jep.2016.04.016. [Epub ahead of print]
BACKGROUND: Fibrinolysis prevents blood clots from growing and becoming problematic. Antifibrinolytics are used as inhibitors of fibrinolysis. Aprotinin was abandoned after identification of major side effects, especially on kidney. Lysine analogues has their own defects and whether they are adequate substitutes for aprotinin is still under doubt. Lamiophlomis rotata (Benth.) Kudo. was previous found to have hemostatic activity. But the active compound in L. rotata and its hemostatic mechanism were unknown.
2.Biological and Enzymatic Characterization of Proteases from Crude Venom of the Ant Odontomachus bauri.
Silva MF1, Mota CM2, Miranda Vdos S3, Cunha Ade O4, Silva MC5, Naves KS6, de Oliveira F7,8, Silva DA9, Mineo TW10, Santiago FM11. Toxins (Basel). 2015 Nov 30;7(12):5114-28. doi: 10.3390/toxins7124869.
Hymenoptera venoms constitute an interesting source of natural toxins that may lead to the development of novel therapeutic agents. The present study investigated the enzymatic and biological characteristics of the crude venom of the ant Odontomachus bauri. Its crude venom presents several protein bands, with higher staining for six proteins with gelatinolytic activity (17, 20, 26, 29, 43 and 48 kDa). The crude venom showed high proteolytic activity on azocasein at optimal pH 8.0 and 37 °C. In the presence of protease inhibitors as aprotinin, leupeptin and EDTA, the azocaseinolytic activity was reduced by 45%, 29% and 9%, respectively, suggesting that the enzymes present in the crude venom belong to the three classes of proteases, with the serine proteases in greater intensity. The crude venom degraded the fibrinogen α-chain faster than the β-chain, while the fibrinogen γ-chain remained unchanged. In biological assays, O. bauri venom showed hemolytic and coagulant activity in vitro, and defibrinating activity in vivo.
3.(99m) Tc-aprotinin - optimisation and validation of radiolabelling kits for routine preparation for diagnostic imaging of amyloidosis.
Denholt C1, Gillings N1. J Labelled Comp Radiopharm. 2016 Apr;59(4):171-4. doi: 10.1002/jlcr.3381. Epub 2016 Feb 28.
Technetium-99m aprotinin was prepared from an optimised radiolabelling kit formulation containing aprotinin, alkaline buffer and stannous chloride (reducing agent) and radiolabelled using (99m) Tc-pertechnetate. The labelling was achieved within 25 min, with radiochemical purities of >98%.
4.Contribution of the Kallikrein/Kinin System to the Mediation of ConA-Induced Inflammatory Ascites.
Baintner K1. Acta Microbiol Immunol Hung. 2016 Mar;63(1):131-7. doi: 10.1556/030.63.2016.1.10.
Intraperitoneal administration of concanavalin A (ConA, 25 mg/kg b.w.), a cell-binding plant lectin was used for inducing inflammatory ascites, and potential inhibitors were tested in 1 h and 2.5 h experiments, i.e. still before the major influx of leucocytes. At the end of the experiment the peritoneal fluid was collected and measured. The ConA-induced ascites was significantly (p<0.01) and dose-dependently inhibited by icatibant (HOE-140), a synthetic polypeptide antagonist of bradykinin receptors. Aprotinin, a kallikrein inhibitor protein also had significant (p<0.01), but less marked inhibitory effect. L-NAME, an inhibitor of NO synthesis, and atropine methylnitrate, an anticholinergic compound, were ineffective. It is concluded, that the kallikrein/kinin system contributes to the mediation of the ConA-induced ascites by increasing subperitoneal vascular permeability, independent of the eventual vasodilation produced by NO. It is known, that membrane glycoproteins are aggregated by the tetravalent ConA and the resulting distortion of membrane structure may explain the activation of the labile prekallikrein.
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