Aprotinin [9087-70-1]

Katalog-Nummer HY-P0017-10mg

Size : 10mg

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Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)

Mass
=
Concentration
×
Volume
×
Molecular Weight *

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start)

C1

×
Volume (start)

V1

=
Concentration (final)

C2

×
Volume (final)

V2

In Vivo:

For the following dissolution methods, please prepare the working solution directly. It is recommended to prepare fresh solutions and use them promptly within a short period of time.
The percentages shown for the solvents indicate their volumetric ratio in the final prepared solution. If precipitation or phase separation occurs during preparation, heat and/or sonication can be used to aid dissolution.

  • Protocol 1

    Add each solvent one by one:  PBS

    Solubility: 50 mg/mL (7.68 mM); Clear solution; Need ultrasonic

In Vivo Dissolution Calculator
Please enter the basic information of animal experiments:

Dosage

mg/kg

Animal weight
(per animal)

g

Dosing volume
(per animal)

μL

Number of animals

Recommended: Prepare an additional quantity of animals to account for potential losses during experiments.
Calculation results:
Working solution concentration: mg/mL
This product has good water solubility, please refer to the measured solubility data in water/PBS/Saline for details.
The concentration of the stock solution you require exceeds the measured solubility. The following solution is for reference only.If necessary, please contact MedChemExpress (MCE).
  • [1]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62.  [Content Brief]

    [2]. Fritz H, et al. Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs. Arzneimittelforschung. 1983;33(4):479-94.  [Content Brief]

    [3]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62.

    [4]. Venturini G, et al. Aprotinin, the first competitive protein inhibitor of NOS activity. Biochem Biophys Res Commun. 1998 Aug 10;249(1):263-5  [Content Brief]

    [5]. Sperzel M, et al. Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J Thromb Haemost. 2007 Oct;5(10):2113-8. Epub 2007 Jul 31.  [Content Brief]

    [6]. Davis R, et al. Aprotinin. A review of its pharmacology and therapeutic efficacy in reducing blood loss associated withcardiac surgery. Drugs. 1995 Jun;49(6):954-83.  [Content Brief]

    [7]. Sabbagh MJ, et al. Aprotinin exacerbates left ventricular dysfunction after ischemia/reperfusion in mice lacking tumor necrosis factor receptor I. J Cardiovasc Pharmacol. 2008 Oct;52(4):355-62.  [Content Brief]

Rats: Male Wistar rats (180-220 g) are used in the study. Aprotinin is dissolved in physiological saline. Aprotinin is administered by bolus injection followed by a maintenance infusion. The doses given are 1.5 mg kg-1 and 3 mg kg-1 h-1, 3mg kg-1 and 6 mg kg-1 h-1 up to 5 mg kg-1 and 10 mg kg-1 h-1. Plasma concentrations for the two agents are assessed by pharmacokinetic studies in rats.

Mice: An intact mouse model of ischemia/reperfusion (30 min-I/60 min-R) is used and left ventricular peak + dP/dt is measured in wild type mice (WT, C57BL/6; n=10), WT mice with aprotinin (4mL/kg; n=10), transgenic mice devoid of the TNFRI (TNFRInull; n=10), and TNFRInull with aprotinin (n=10).

MCE hat die Genauigkeit dieser Methoden nicht unabhängig bestätigt. Sie dienen nur als Referenz.

  • [1]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62.  [Content Brief]

    [2]. Fritz H, et al. Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs. Arzneimittelforschung. 1983;33(4):479-94.  [Content Brief]

    [3]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62.

    [4]. Venturini G, et al. Aprotinin, the first competitive protein inhibitor of NOS activity. Biochem Biophys Res Commun. 1998 Aug 10;249(1):263-5  [Content Brief]

    [5]. Sperzel M, et al. Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J Thromb Haemost. 2007 Oct;5(10):2113-8. Epub 2007 Jul 31.  [Content Brief]

    [6]. Davis R, et al. Aprotinin. A review of its pharmacology and therapeutic efficacy in reducing blood loss associated withcardiac surgery. Drugs. 1995 Jun;49(6):954-83.  [Content Brief]

    [7]. Sabbagh MJ, et al. Aprotinin exacerbates left ventricular dysfunction after ischemia/reperfusion in mice lacking tumor necrosis factor receptor I. J Cardiovasc Pharmacol. 2008 Oct;52(4):355-62.  [Content Brief]

  • [1]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62.

    [2]. Fritz H, et al. Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs. Arzneimittelforschung. 1983;33(4):479-94.

    [3]. Levy JH, et al. Efficacy and safety of aprotinin in cardiac surgery. Orthopedics. 2004 Jun;27(6 Suppl):s659-62.

    [4]. Venturini G, et al. Aprotinin, the first competitive protein inhibitor of NOS activity. Biochem Biophys Res Commun. 1998 Aug 10;249(1):263-5

    [5]. Sperzel M, et al. Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J Thromb Haemost. 2007 Oct;5(10):2113-8. Epub 2007 Jul 31.

    [6]. Davis R, et al. Aprotinin. A review of its pharmacology and therapeutic efficacy in reducing blood loss associated withcardiac surgery. Drugs. 1995 Jun;49(6):954-83.

    [7]. Sabbagh MJ, et al. Aprotinin exacerbates left ventricular dysfunction after ischemia/reperfusion in mice lacking tumor necrosis factor receptor I. J Cardiovasc Pharmacol. 2008 Oct;52(4):355-62.

Optional Solvent Concentration Solvent Mass 1 mg 5 mg 10 mg 25 mg
DMSO / H2O 1 mM 0.1536 mL 0.7679 mL 1.5358 mL 3.8394 mL
5 mM 0.0307 mL 0.1536 mL 0.3072 mL 0.7679 mL
10 mM 0.0154 mL 0.0768 mL 0.1536 mL 0.3839 mL
H2O 15 mM 0.0102 mL 0.0512 mL 0.1024 mL 0.2560 mL

* Note: If you choose water as the stock solution, please dilute it to the working solution, then filter and sterilize it with a 0.22 μm filter before use.

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  • Anti-infection Metabolic Enzyme/Protease
  • Influenza Virus Ser/Thr Protease
Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

Keywords:

Aprotinin9087-70-1Influenza VirusSer/Thr ProteaseSerine proteasesSerine endopeptidasesThreonine proteasesInhibitorinhibitorinhibit

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Aprotinin
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HY-P0017
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