176900 Anthrax Lethal Factor, Recombinant, Bacillus anthracis, B. anthracis - Calbiochem

176900
Price could not be retrieved
Minimum Quantity needs to be mulitiple of
Upon Order Completion More Information
You Saved ()
 
Request Pricing
Limited AvailabilityLimited Availability
In Stock 
Discontinued
Limited Quantities Available
Availability to be confirmed
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      Contact Customer Service
      View Pricing & Availability
      Click To Print This Page

      Overview

      Replacement Information

      Key Spec Table

      Pricing & Availability

      Catalogue NumberAvailability Packaging Qty/Pack Price Quantity
      US1176900-100UG
      Retrieving availability...
      Limited AvailabilityLimited Availability
      In Stock 
      Discontinued
      Limited Quantities Available
      Availability to be confirmed
        Remaining : Will advise
          Remaining : Will advise
          Will advise
          Contact Customer Service
          Contact Customer Service

          Plastic ampoule 100 μg
          Retrieving price...
          Price could not be retrieved
          Minimum Quantity needs to be mulitiple of
          Upon Order Completion More Information
          You Saved ()
           
          Request Pricing
          Description
          OverviewRecombinant, Bacillus anthracis anthrax lethal factor expressed in a specialized strain of B. anthracis. One of the three protein components of Anthrax toxin, lethal factor (LF) is a highly specific protease that cleaves members of the mitogen-activated protein kinase kinase (MAPKK) family. LF is comprised of four domains. Domain I binds the protective antigen to enter the target cell; domains II, III, and IV create a long groove to hold and cleave the MAPKK proteins.
          Catalogue Number176900
          Brand Family Calbiochem®
          References
          ReferencesBrossier, F., and Mock, M. 2001. Toxicon 39, 1747.
          Friedlander, A.M. 2001. Nature 414, 160.
          Gupta, P., et al. 2001. Biochem. Biophys. Res. Commun. 284, 568.
          Pannifer, A.D., et al. 2001. Nature 414, 160.
          Pugsley, A.P. 1996. Proc. Natl. Acad. Sci. USA 93, 8155.
          Leppla, S.H. 1991. Methods Enzymol. 195, 153.
          Product Information
          Unit of DefinitionOne unit is defined as the amount of enzyme required to catalyze the release of 1.0 pmole of cleaved MAPKKide™ substrate per min at 37°C, in 20 mM HEPES, pH 8.2.
          FormLyophilized
          FormulationLyophilized from 50 mM NaCl, 5 mM HEPES, pH 7.5.
          Applications
          Biological Information
          Primary TargetMAPKK
          PuritySingle major band by SDS-PAGE
          Physicochemical Information
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Ambient Temperature Only
          Toxicity Standard Handling
          Storage +2°C to +8°C
          Do not freeze Ok to freeze
          Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 6 months at -20°C.
          End use certificateY
          Canadian export regulations Due to the country and/or U.S. state of origin of the animal material used in this product, this product may not be exported to Canada.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          Certificates of Analysis

          TitleLot Number
          176900

          References

          Reference overview
          Brossier, F., and Mock, M. 2001. Toxicon 39, 1747.
          Friedlander, A.M. 2001. Nature 414, 160.
          Gupta, P., et al. 2001. Biochem. Biophys. Res. Commun. 284, 568.
          Pannifer, A.D., et al. 2001. Nature 414, 160.
          Pugsley, A.P. 1996. Proc. Natl. Acad. Sci. USA 93, 8155.
          Leppla, S.H. 1991. Methods Enzymol. 195, 153.
          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.

          Revision14-October-2013 JSW
          DescriptionRecombinant, Bacillus anthracis anthrax lethal factor expressed in a special strain of B. anthracis. One of three protein components of anthrax toxin produced by the pathogenic bacterium, Bacillus anthracis. Highly specific protease component that cleaves members of the mitogen-activated protein kinase kinase (MAPKK) family. LF is comprised of four domains: domain I that binds to protective antigen (necessary for entry into the cellular target) and domains II, III, and IV which form a long groove to hold and cleave the target proteins. Requires passage through an acidic vesicle prior to translocation to the cytoplasm of the cell. Cleavage of target proteins leads to the inhibition of multiple signaling pathways and cell death.
          FormLyophilized
          FormulationLyophilized from 50 mM NaCl, 5 mM HEPES, pH 7.5.
          PuritySingle major band by SDS-PAGE
          Unit definitionOne unit is defined as the amount of enzyme required to catalyze the release of 1.0 pmole of cleaved MAPKKide™ substrate per min at 37°C, in 20 mM HEPES, pH 8.2.
          SolubilityPlease refer to the vial label for lot-specific reconstitution volume.
          Storage +2°C to +8°C
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Avoid freeze/thaw cycles of solutions. Stock solutions are stable for up to 6 months at -20°C.
          Toxicity Standard Handling
          ReferencesBrossier, F., and Mock, M. 2001. Toxicon 39, 1747.
          Friedlander, A.M. 2001. Nature 414, 160.
          Gupta, P., et al. 2001. Biochem. Biophys. Res. Commun. 284, 568.
          Pannifer, A.D., et al. 2001. Nature 414, 160.
          Pugsley, A.P. 1996. Proc. Natl. Acad. Sci. USA 93, 8155.
          Leppla, S.H. 1991. Methods Enzymol. 195, 153.