342001 Procathepsin K, Human, Recombinant, E. coli

342001
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      342001-10UG
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          Plastic ampoule 10 μg
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          Description
          OverviewRecombinant, human procathepsin K (amino acids 19-329) (GenBank target symbol = S79895, ACC No. P43235) expressed in E. coli with a methionine residue inserted at amino acid 18 to create a new N-terminal initiation site. Cathepsin K, a member of the papain superfamily of cysteine proteinases, plays an important role in osteoclast-mediated bone resorption and collagen degradation. Cathepsin K is synthesized as an inactive proenzyme that is converted to its mature, active form by proteolytic cleavage of the 99 amino acid propeptide domain. Inhibitors of cathepsin K include leupeptin (Cat. No. 108975) (IC50 = 70 nM), E-64 (Cat. No. 324890) (IC50 = 5 nM), and cystatin (Cat. No. 324891 or 324896). Requires activation prior to use.
          Note: 1 mU = 1 milliunit.
          If the activated enzyme is not used immediately, it is recommended to add methyl methanthiosulfonate (1 mM final concentration MMTS).
          Catalogue Number342001
          Brand Family Calbiochem®
          References
          ReferencesMcQueney, M., et al. 1997. J. Bio. Chem. 272, 13955.
          Bossard, M., et al. 1996. J. Biol. Chem. 271, 12517.
          Drake, F., et al. 1996. J. Biol. Chem. 271, 12511.
          Bromme, D. and Okamoto, K. 1995. Biol. Chem. Hoppe-Seyler 376, 379.
          Baron, R. 1989 Anat. Rec. 224, 317.
          Littlewood-Evans, A.J., et al. 1975. Cancer Res. 57, 5386.
          Nishimura, J.S. et al. 1975. Arch. Biochem. Biophys. 170, 461.
          Product Information
          Activity≥1000 mU/mg protein
          Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmole benzyloxycarbonyl-phenylalanine-arginine-7-amido-4-methylcoumarin per min at 37°C, pH 5.5.
          EC number3.4.22.38
          FormLiquid
          FormulationIn 500 mM NaCl, 25 mM Tris, pH 8.0.
          Applications
          Biological Information
          Purity≥95% by SDS-PAGE
          Concentration Label Please refer to vial label for lot-specific concentration
          Physicochemical Information
          Dimensions
          Materials Information
          Toxicological Information
          Safety Information according to GHS
          Safety Information
          Product Usage Statements
          Storage and Shipping Information
          Ship Code Dry Ice Only
          Toxicity Standard Handling
          Storage ≤ -70°C
          Avoid freeze/thaw Avoid freeze/thaw
          Do not freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C). Following activation the enzyme is unstable and should include MMTS for storage (see recommended reaction conditions for activation).
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          342001

          References

          Reference overview
          McQueney, M., et al. 1997. J. Bio. Chem. 272, 13955.
          Bossard, M., et al. 1996. J. Biol. Chem. 271, 12517.
          Drake, F., et al. 1996. J. Biol. Chem. 271, 12511.
          Bromme, D. and Okamoto, K. 1995. Biol. Chem. Hoppe-Seyler 376, 379.
          Baron, R. 1989 Anat. Rec. 224, 317.
          Littlewood-Evans, A.J., et al. 1975. Cancer Res. 57, 5386.
          Nishimura, J.S. et al. 1975. Arch. Biochem. Biophys. 170, 461.
          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.

          Revision27-September-2007 RFH
          DescriptionRecombinant, human procathepsin K (amino acids 19-329) (GenBank target symbol = S79895, ACC No. P43235) expressed in E. coli with a methionine residue inserted at amino acid 18 to create a new N-terminal initiation site. Cathepsin K, a member of the papain superfamiliy of cysteine proteinases, plays an important role in osteoclast-mediated bone resorption and collagen degradation. Cathepsin K is synthesized as an inactive proenzyme that is converted to its mature, active form by proteolytic cleavage of the 99 amino acid propeptide domain. Inhibitors of cathepsin K include leupeptin (Cat. No. 108975) (IC50 = 70 nM), E-64 (Cat. No. 324890) (IC50 = 5 nM), and cystatin (Cat. No. 324891 or 324896). Requires activation prior to use.
          FormLiquid
          FormulationIn 500 mM NaCl, 25 mM Tris, pH 8.0.
          Concentration Label Please refer to vial label for lot-specific concentration
          Recommended reaction conditions
          Activation 1. Add an equal volume of 100 mM sodium acetate buffer, 10 mM DTT, 5 mM EDTA, pH 3.9 and incubate at room temperature for 40 min. This will adjust the pH of the procathepsin K to 4.0. 2. If the activated enzyme is not to be used immediately, add methyl methanthiosulfonate (MeS-SO2Me; MMTS) to a final concentration of 1 mM. Aliquot, flash-freeze in liquid nitrogen, and freeze at -70°C. MMTS is a hydrophobic, thiol-reactive compound that modifies cysteines by attaching the uncharged thiomethyl-blocking group to reactive sulhydryl groups. This is a reversible reaction that arrests autoproteolysis. The activity of the enzyme can be restored to (near) unmodified levels by adding an excess of L-cysteine (~3 molar excess over MMTS). Activity Activated cathepsin K activity can be measured in 50 mM MES, 5 mM DTT, 2.5 mM EDTA, pH 5.5, and 100 µM benzyloxycarbonyl-phenylalanine-arginine-7-amido-4-methylcoumarin. Fluorescence is monitored at an excitation wavelength of ~360 nm and an emission wavelength of ~460 nm. To quantitate enzyme activity a 7-amino-4-methylcoumarin standard curve (100-5000 pmol) should be included with each assay. (Note: if MMTS was added to the enzyme after activation, the reaction buffer should also include 3 mM L-cysteine).
          EC number3.4.22.38
          Purity≥95% by SDS-PAGE
          Activity≥1000 mU/mg protein
          Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmole benzyloxycarbonyl-phenylalanine-arginine-7-amido-4-methylcoumarin per min at 37°C, pH 5.5.
          Storage ≤ -70°C
          Avoid freeze/thaw
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C). Following activation the enzyme is unstable and should include MMTS for storage (see recommended reaction conditions for activation).
          Toxicity Standard Handling
          ReferencesMcQueney, M., et al. 1997. J. Bio. Chem. 272, 13955.
          Bossard, M., et al. 1996. J. Biol. Chem. 271, 12517.
          Drake, F., et al. 1996. J. Biol. Chem. 271, 12511.
          Bromme, D. and Okamoto, K. 1995. Biol. Chem. Hoppe-Seyler 376, 379.
          Baron, R. 1989 Anat. Rec. 224, 317.
          Littlewood-Evans, A.J., et al. 1975. Cancer Res. 57, 5386.
          Nishimura, J.S. et al. 1975. Arch. Biochem. Biophys. 170, 461.