Antipain (hydrochloride)
(Synonyms: 抗痛素二盐酸盐) 目录号 : GC40032A protease inhibitor
Cas No.:37682-72-7
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
Antipain is a protease inhibitor originally isolated from actinomycetes.[1] It inhibits thrombokinase, plasmin, trypsin, and papain in vitro (IC50s = 20, 93, 0.26, and 0.16 μg/ml, respectively). Antipain (6-600 μg/ml) inhibits the morphological transformation of and increases frequency of chromosomal aberrations in Syrian hamster embryo cells induced by N-methyl-N'-nitro-N-nitroso-guanidine (MNNG).[2] In vivo, antipain (25-100 mg/kg) suppresses urethan-induced formation of cleft palates and cleft lips in mice.[3]
Reference:
[1]. Suda, H., Aoyagi, T., Hamada, M., et al. Antipain, a new protease inhibitor isolated from actinomycetes. J. Antibiot. (Tokyo) 25(4), 263-266 (1972).
[2]. DiPaolo, J.A., Amsbaugh, S.C., and Popescu, N.C. Antipain inhibits N-methyl-N'-nitro-N-nitrosoguanidine-induced transformation and increases chromosomal aberrations. Proc. Natl. Acad. Sci. U.S.A. 77(11), 6649-6653 (1980).
[3]. Nomura, T., Enomoto, T., Shibata, K., et al. Antiteratogenic effects of tumor inhibitors, caffeine, antipain, and retinoic acid in mice. Cancer Res. 43(11), 5156-5162 (1983).
| Cas No. | 37682-72-7 | SDF | |
| 别名 | 抗痛素二盐酸盐 | ||
| 化学名 | N2-[[[(1S)-1-carboxy-2-phenylethyl]amino]carbonyl]-L-arginyl-N-[4-[(aminoiminomethyl)amino]-1-formylbutyl]-L-valinamide, dihydrochloride | ||
| Canonical SMILES | O=C(O)C(NC(N[C@@H](CCCNC(N)=N)C(N[C@@H](C(C)C)C(NC(C=O)CCCNC(N)=N)=O)=O)=O)CC1=CC=CC=C1.Cl.Cl | ||
| 分子式 | C27H44N10O6 • 2HCl | 分子量 | 677.6 |
| 溶解度 | Soluble in ethanol, DMSO, also soluble in water | 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 | 1.4758 mL | 7.379 mL | 14.758 mL |
| 5 mM | 0.2952 mL | 1.4758 mL | 2.9516 mL |
| 10 mM | 0.1476 mL | 0.7379 mL | 1.4758 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 PLGA-PEG-PLGA Thermosensitive Gel Enabling Sustained Delivery of Ropivacaine hydrochloride for Postoperative Pain Relief
Chem Pharm Bull (Tokyo) 2017;65(3):229-235.PMID:28250344DOI:10.1248/cpb.c16-00471.
Postoperative pain is a complex physiological response to disease and tissue injury. Moderate-to-severe pain typically occurs within 48 h after surgery. Amino amide local anesthetics are widely applied to manage postoperative pain, and they have high efficacy, a low risk for addiction and limited side effects. However, these anesthetics also have short half-lives, often necessitating continuous injection to obtain satisfactory pain relief. In the current work, we used a poly(lactic-co-glycolic acid) (PLGA)-polyethylene glycol (PEG)-PLGA (PLGA-PEG-PLGA) temperature-sensitive gel to deliver a local anesthetic, ropivacaine hydrochloride (RP), to prolong its analgesic effect. We investigated the influence of polymer and drug concentration on gelation temperature and the in vitro drug release rate from the temperature-sensitive gel. RP-loaded PLGA-PEG-PLGA solution is a liquid at room temperature and forms a gel at temperatures slightly lower than body temperature. With regard to the gel's drug release rate, 37.5, 51.3 and 72.6% of RP was released at 12, 24 and 48 h, respectively. This in vitro drug release profile conformed to the Higuchi equation. To assess pain control efficacy when using the gel, we evaluated the mechanical paw withdrawal reflex threshold, thermal pain threshold and incision cumulative pain scores in a rat incisional model. The results showed that the anti-pain effect of a single injection of RP-loaded gel at the incision site lasted for 48 h, which is significantly longer than the effect produced by injection of RP solution alone. The use of RP-loaded thermosensitive gels could provide a promising method for managing postoperative pain.
Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors
Acta Pharmacol Sin 2003 Sep;24(9):923-9.PMID:12956943doi
Aim: To investigate the actions of protease inhibitors on the enzymatic activities of tryptase and chymase in similar experimental systems. Methods: Human lung tryptase and human skin chymase were purified by a similar procedure involving high salt extraction of tryptase, heparin agarose affinity chromatography, and S-200 Sephacryl gel filtration chromatography. Actions of protease inhibitors on tryptase and chymase activities were examined by enzyme assays. Results: The specific activities of tryptase and chymase were 2.1 kU/g protein and 4.9 kU/g protein, respectively. Both preparations showed a single diffuse band on SDS-PAGE. Among non-native protease inhibitors, N-(1-hydroxy-2-naphthoyl)-L- arginyl-L-prolinamide hydrochloride (HNAP), leupeptin, Antipain, benzamidine, and protamine inhibited more than 90 % enzymatic activity of tryptase, whereas soy bean trypsin inhibitor (SBTI), Z-Ile-Glu-Pro-Phe-CO2Me (ZIGPPM) and chymostatin inhibited more than 95 % enzymatic activity of chymase. Native protease inhibitors alpha 1-antitrypsin and secretory leukocyte protease inhibitor (SLPI) inhibited more than 90 % enzymatic activity of chymase, but lactoferrin appeared to enhance chymase enzymatic activity. All the 3 inhibitors had weak inhibitory actions on tryptase. Conclusion: The protease inhibitors tested had relatively good selectivity to either tryptase or chymase.
Spinesin/TMPRSS5, a novel transmembrane serine protease, cloned from human spinal cord
J Biol Chem 2002 Mar 1;277(9):6806-12.PMID:11741986DOI:10.1074/jbc.M103645200.
A cDNA encoding a novel serine protease, which we designated spinesin, has been cloned from human spinal cord. The longest open reading frame was 457 amino acids. A homology search revealed that the human spinesin gene was located at chromosome 11q23 and contained 13 exons, the gene structure being similar to that of TMPRSS3 whose gene is also located on 11q23. Spinesin has a simple type II transmembrane structure, consisting of, from the N terminus, a short cytoplasmic domain, a transmembrane domain, a stem region containing a scavenger receptor-like domain, and a serine protease domain. Unlike TMPRSS3, it carries no low density lipoprotein receptor domain in the stem region. The extracellular region carries five N-glycosylation sites. The sequence of the protease domain carried the essential triad His, Asp, and Ser and showed some similarity to that of TMPRSS2, hepsin, HAT, MT-SP1, TMPRSS3, and corin, sharing 45.5, 41.9, 41.3, 40.3, 39.1, and 38.5% identity, respectively. The putative mature protease domain preceded by H(6)DDDDK was produced in Escherichia coli, purified, and successfully activated by immobilized enterokinase. Its optimal pH was about 10. It cleaved synthetic substrates for trypsin, which is inhibited by p-amidinophenylmethanesulfonyl fluoride hydrochloride but not by Antipain or leupeptin. Northern blot analysis against mRNA from human tissues including liver, lung, placenta, and heart demonstrated a specific expression of spinesin mRNA in the brain. Immunohistochemically, spinesin was predominantly expressed in neurons, in their axons, and at the synapses of motoneurons in the spinal cord. In addition, some oligodendrocytes were clearly stained. These results indicate that spinesin is transported to the synapses through the axons after its synthesis in the cytoplasm and may play important roles at the synapses. Further analyses are required to clarify its roles at the synapses and in oligodendrocytes.
Identification of a serine protease as a major allergen (Per a 10) of Periplaneta americana
Allergy 2008 Jun;63(6):768-76.PMID:18445191DOI:10.1111/j.1398-9995.2007.01602.x.
Background: Cockroach allergens are associated with the development of asthma, but none of these has been characterized for proteolytic activity. This study was undertaken to isolate and characterize a protease from Periplaneta americana and determine its allergenicity. Methods: A serine protease was isolated from P. americana extract using benzamidine sepharose column and characterized by immunobiochemical methods. Allergenicity of the protease was assessed by enzyme-linked immunosorbent assay, immunoblot, intradermal testing, histamine release and peripheral blood mononuclear cells (PBMCs) proliferation. Results: Affinity purified protein of approximately 28 kDa (Per a 10) showed a single band of activity in gelatin zymogram and agarose plate assay. N-terminal sequence (IVGGRPAQI) revealed similarity with mite serine protease allergens and insect trypsins. It demonstrated proteolytic activity with azocollagen > gelatin > defatted-milk > casein including serine protease specific substrate, N-benzoyl-arginine-ethyl-ester-hydrochloride. It was inhibited by serine protease inhibitors, namely aprotinin > pefabloc > AEBSF > PMSF > benzamidine > Antipain > leupeptin and trypsin-specific inhibitor (tosyl-lysyl-chloromethyl-ketone) suggesting it to be a trypsin-like serine protease. Per a 10 was recognized as a major allergen, showing IgE reactivity with >80% of cockroach sensitized patients by skin tests and immunoblot. It could induce significant histamine release (P < 0.05) in blood and secretion of interleukin-4 (IL-4) (P < 0.05) and IL-5 (P < 0.05) in culture supernatant of PBMCs from cockroach hypersensitive patients, suggesting a strong allergenic potency. Conclusion: A serine protease isolated from P. americana was demonstrated to be a major allergen (Per a 10). It has a potential for component-based diagnosis of allergy and will be useful in elucidating the mechanism of allergy.
Characterization of soybean trypsin inhibitor sensitive protease from unfertilized sea urchin eggs
Biochemistry 1985 Jul 16;24(15):3926-31.PMID:3902077DOI:10.1021/bi00336a018.
A serine protease from sea urchin eggs has been isolated by affinity chromatography on soybean trypsin inhibitor-agarose. Benzamidine hydrochloride was included to minimize autodegradation. We present data on the properties of the protease with respect to molecular weight and its interaction with trypsin inhibitors and substrates. The molecular weight of the enzyme is 47 000 by gel filtration under nonreducing conditions and 35 000 by electrophoresis in the presence of sodium dodecyl sulfate and dithiothreitol. The pH optimum and Km with N alpha-benzoyl-L-arginine ethyl ester (BAEE) are 8.0 and 75 microM, respectively. The specific activity is comparable to that of bovine pancreatic trypsin. Proteolytic activity was measured by beta-casein hydrolysis. The caseinolytic activity is completely inhibited by 1 mumol of soybean trypsin inhibitor (SBTI) per micromole of enzyme. BAEE esterase activity is inhibited competitively by SBTI (Ki = 1.6 nM), lima bean trypsin inhibitor (150 nM), chicken ovomucoid (100 nM), and leupeptin (130 nM). Bowman-Birk inhibitor, benzamidine hydrochloride, and Antipain are also inhibitors of the purified enzyme. Inhibition by phenylmethanesulfonyl fluoride and N alpha-p-tosyl-L-lysine chloromethyl ketone indicates the presence of serine and histidine residues in the active center, respectively. The chymotrypsin inhibitor L-1-(tosylamido)-2-phenylethyl chloromethyl ketone is ineffective. The protease is susceptible to autodegradation which can result in the appearance of a minor 23-kilodalton component. The egg protease appears to be similar in many respects to trypsins and trypsin-like enzymes isolated from a wide variety of sources, including sea urchin and mammalian sperm.