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616370 Aprotinin, Bovine Lung, Crystalline - CAS 9087-70-1 - Calbiochem

Overview

Replacement Information

Key Specifications Table

CAS #
9087-70-1

Products

Catalog NumberPackaging Qty/Pack
616370-100MG Plastic ampoule 100 mg
616370-10MG Plastic ampoule 10 mg
616370-20MG Plastic ampoule 20 mg
Description
OverviewA competitive and reversible inhibitor of esterases and proteases. Forms a tight complex with and blocks the active site of the enzymes. Inhibits a number of different proteases, including chymotrypsin, coagulation factors involved in the prephase of blood clotting, kallikrein (Kd = 1 x 10-7 M), plasmin (Kd = 2.3 x 10-10 M) , tissue and leukocytic proteinases, and trypsin (Kd = 5 x 10-14 M). Does not inhibit Factor Xa and thrombin. It is relatively acid- and heat-stable. Useful as a serine protease inhibitor during purification of proteins and in studies of zymogen activation systems. Reported to suppress virus HA cleavage and limit reproduction of human and avian influenza viruses with a single arginine in the HA cleavage site.
Effectively inhibits target proteases at equimolar concentration.
Note: 1 KIU = 0.025 antiplasmin units (APU) = 0.0016 trypsin inhibitor units (using porcine trypsin) = 0.0009756 trypsin inhibitor units (using bovine trypsin).
Catalogue Number616370
Brand Family Calbiochem®
SynonymsPancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor
References
ReferencesZhirnov, O.P., et al. 2011. Antiviral Res. 92, 27.
Roberts, R.F., et al. 1998. Ann. Thorac. Surg. 66, 225.
Azougagh Oualane, F., et al. 1992. Thromb. Res. 68, 185.
Anderson, L.O., et al. 1986. Proc. Natl. Acad. Sci. USA 83, 2979.
Kruithof, W.L., et al. 1986. Biochem. J. 226, 631.
McKeehan, W.L., et al. 1986. J. Biol. Chem. 261, 5378.
Fritz, H., and Wunderer, G. 1983. Arzneim. Forsch. 33, 479.
Rijken, D.C., and Collen, D. 1981. J. Biol. Chem. 256, 7035.
Kassell, B., et al. 1970. Methods Enzymol. 19, 845.
Product Information
CAS number9087-70-1
Activity≥5500 KIU/mg dry weight
Unit of DefinitionOne Kallikrein Inhibitory Unit (K.I.U.) is defined as the quantity of protease inhibitor that will inhibit two kallikrein units by 50% under optimal conditions. Note: 1 KIU = 0.025 antiplasmin units (APU) or 0.0031 trypsin inhibitor units.
ATP CompetitiveN
FormWhite to off-white crystalline solid
Hygroscopic Hygroscopic
PI10.5
ReversibleY
Quality LevelMQ200
Applications
Biological Information
Primary Targetchymotrypsin
Primary Target IC<sub>50</sub>Kd = 1 x 10-7 M, 2.3 x 10-10 M, 5 x 10-14 M, against kallikrein, plasmin, and trypsin, respectively
Purity≥95% by gel filtration
Physicochemical Information
Cell permeableN
Contaminantsendotoxin: ≤10 EU/mg
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
RTECSYN5080000
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage +2°C to +8°C
Hygroscopic Hygroscopic
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution refrigerate (4°C). Stock solutions are stable for up to 3 months at 4°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
616370-100MG 04055977262889
616370-10MG 07790788056292
616370-20MG 04055977262896

Documentation

Aprotinin, Bovine Lung, Crystalline - CAS 9087-70-1 - Calbiochem SDS

Title

Safety Data Sheet (SDS) 

Aprotinin, Bovine Lung, Crystalline - CAS 9087-70-1 - Calbiochem Certificates of Analysis

TitleLot Number
616370

References

Reference overview
Zhirnov, O.P., et al. 2011. Antiviral Res. 92, 27.
Roberts, R.F., et al. 1998. Ann. Thorac. Surg. 66, 225.
Azougagh Oualane, F., et al. 1992. Thromb. Res. 68, 185.
Anderson, L.O., et al. 1986. Proc. Natl. Acad. Sci. USA 83, 2979.
Kruithof, W.L., et al. 1986. Biochem. J. 226, 631.
McKeehan, W.L., et al. 1986. J. Biol. Chem. 261, 5378.
Fritz, H., and Wunderer, G. 1983. Arzneim. Forsch. 33, 479.
Rijken, D.C., and Collen, D. 1981. J. Biol. Chem. 256, 7035.
Kassell, B., et al. 1970. Methods Enzymol. 19, 845.

Citations

Title
  • Zhirnov, O.P., et al. 2011. Antiviral Res. 92, 27.
  • Data Sheet

    Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

    Revision28-February-2012 RFH
    SynonymsPancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor
    DescriptionA competitive and reversible inhibitor of esterase and protease activity. Forms a tight complex with and blocks the active site of target enzymes. Inhibits a number of different proteases, including chymotrypsin, coagulation factors involved in the pre-phase of blood clotting, kallikrein (Kd = 1 X 10-7 M), plasmin (Kd = 2.3 X 10-10 M), tissue and leukocyte proteinases, and trypsin (Kd = 5 X 10-14 M). Does not inhibit Factor Xa or thrombin. Reported to be relatively acid and heat stable. Effectively inhibits target proteases at equimolar concentration. Useful as a serine proteinase inhibitor during purification of proteins and in studies of zymogen activation systems. Reported to suppress virus HA cleavage and limit reproduction of human and avian influenza viruses with a single arginine in the HA cleavage site.
    FormWhite to off-white crystalline solid
    CAS number9087-70-1
    RTECSYN5080000
    Purity≥95% by gel filtration
    Contaminantsendotoxin: ≤10 EU/mg
    Activity≥5500 KIU/mg dry weight
    Unit definitionOne Kallikrein Inhibitory Unit (K.I.U.) is defined as the quantity of protease inhibitor that will inhibit two kallikrein units by 50% under optimal conditions. Note: 1 KIU = 0.025 antiplasmin units (APU) or 0.0031 trypsin inhibitor units.
    SolubilityH₂O (10 mg/ml)
    Storage +2°C to +8°C
    Hygroscopic
    Do Not Freeze Ok to freeze
    Special InstructionsFollowing reconstitution refrigerate (4°C). Stock solutions are stable for up to 3 months at 4°C.
    Toxicity Standard Handling
    Merck USA index14, 757
    ReferencesZhirnov, O.P., et al. 2011. Antiviral Res. 92, 27.
    Roberts, R.F., et al. 1998. Ann. Thorac. Surg. 66, 225.
    Azougagh Oualane, F., et al. 1992. Thromb. Res. 68, 185.
    Anderson, L.O., et al. 1986. Proc. Natl. Acad. Sci. USA 83, 2979.
    Kruithof, W.L., et al. 1986. Biochem. J. 226, 631.
    McKeehan, W.L., et al. 1986. J. Biol. Chem. 261, 5378.
    Fritz, H., and Wunderer, G. 1983. Arzneim. Forsch. 33, 479.
    Rijken, D.C., and Collen, D. 1981. J. Biol. Chem. 256, 7035.
    Kassell, B., et al. 1970. Methods Enzymol. 19, 845.
    Citation
  • Zhirnov, O.P., et al. 2011. Antiviral Res. 92, 27.