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317640 Dipeptidyl Peptidase IV (CD26), Porcine Kidney

317640
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317640-250MIU
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      Plastic ampoule 250 miu
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      Description
      OverviewNative, DPP IV purified from porcine kidney (renal brush border of the proximal tubule). A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. Cleaves Xaa-Pro dipeptides from the N-terminus of oligo and polypeptides. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, T cell activation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. MW: ~210000-260000 (unreduced).
      Catalogue Number317640
      Brand Family Calbiochem®
      SynonymsCD26, DPPIV
      References
      ReferencesBar, J., et al. 2003. Biol. Chem. 384, 1553.
      Engel, M., et al. 2003. Proc. Natl. Acad. Sci. USA 100, 5063.
      Ikehara, Y., et al. 1994. Methods. Enzymol. 244, 215.
      David, F., et al. 1993. J. Biol. Chem. 268, 17247.
      Thomsen, P.D., et al. 1993. Mamm. Genome 4, 604.
      Misumi, Y., et al. 1992. Biochim. Biophys. Acta. 1131, 333.
      Seidl, R., et al. 1991. Biol. Chem. Hoppe Seyler 372, 213.
      Checler, F., et al. 1985. J. Neurochem. 45, 1509.
      Imai, K., et al. 1983. J. Biochem. 93, 431.
      Kato, T., et al. 1979. Experientia. 35, 409.
      Kojima, K., et al. 1979. Anal. Biochem. 100, 43.
      Kato, T., et al. 1978. Biochem. Med. 19, 351.
      Kenny, A.J., et al. 1976. Biochem. J. 157, 169.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmole 7-(Gly-Pro)-amino-4-methylcoumarinamide per min at 37°C, pH 8.5.
      EC number3.4.14.5
      FormLiquid
      FormulationIn 20 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% NaN₃, pH 8.0.
      Quality LevelMQ100
      Applications
      Biological Information
      Purity≥90% by SDS-PAGE
      Specific Activity≥35 units/mg protein
      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 InstructionsDilute only the amount of enzyme needed for each assay. Upon thawing, do not re-freeze, store in the refrigerator (4°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Dipeptidyl Peptidase IV (CD26), Porcine Kidney SDS

      Title

      Safety Data Sheet (SDS) 

      Dipeptidyl Peptidase IV (CD26), Porcine Kidney Certificates of Analysis

      TitleLot Number
      317640

      References

      Reference overview
      Bar, J., et al. 2003. Biol. Chem. 384, 1553.
      Engel, M., et al. 2003. Proc. Natl. Acad. Sci. USA 100, 5063.
      Ikehara, Y., et al. 1994. Methods. Enzymol. 244, 215.
      David, F., et al. 1993. J. Biol. Chem. 268, 17247.
      Thomsen, P.D., et al. 1993. Mamm. Genome 4, 604.
      Misumi, Y., et al. 1992. Biochim. Biophys. Acta. 1131, 333.
      Seidl, R., et al. 1991. Biol. Chem. Hoppe Seyler 372, 213.
      Checler, F., et al. 1985. J. Neurochem. 45, 1509.
      Imai, K., et al. 1983. J. Biochem. 93, 431.
      Kato, T., et al. 1979. Experientia. 35, 409.
      Kojima, K., et al. 1979. Anal. Biochem. 100, 43.
      Kato, T., et al. 1978. Biochem. Med. 19, 351.
      Kenny, A.J., et al. 1976. Biochem. J. 157, 169.
      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.

      Revision19-June-2008 RFH
      SynonymsCD26, DPPIV
      DescriptionNative, DPP IV purified from porcine kidney (renal brush border of the proximal tubule). A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. Cleaves Xaa-Pro dipeptides from the N-terminus of oligo and polypeptides. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, T cell activation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. MW: ~210000-260000 (unreduced).
      FormLiquid
      FormulationIn 20 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% NaN₃, pH 8.0.
      Concentration Label Please refer to vial label for lot-specific concentration
      Recommended reaction conditions
      Activity Assay The specific activity can be assayed using the synthetic substrate, 7-(Gly-Pro)-amino-4-methylcoumarinamide, and the cleavage product, 7-amino-4-methylcourmain (AMC). Both are fluorescent, but the excitation/emission spectra are different; at an excitation/emission setting of 380 nm/460 nm, only the AMC product is measured. For quantitative measurement an AMC standard curve should be included; the recommended range is 100-800 pmol. Alternatively, the activity can be measured using the colorimetric substrate, H-Gly-Pro-pNA. The activity is then monitored at 405 nm over a period of time. A standard curve can be generated using 4-nitroaniline in the range of 5-100 nmol.
      EC number3.4.14.5
      Purity≥90% by SDS-PAGE
      Specific activity≥35 units/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmole 7-(Gly-Pro)-amino-4-methylcoumarinamide per min at 37°C, pH 8.5.
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsDilute only the amount of enzyme needed for each assay. Upon thawing, do not re-freeze, store in the refrigerator (4°C).
      Toxicity Standard Handling
      ReferencesBar, J., et al. 2003. Biol. Chem. 384, 1553.
      Engel, M., et al. 2003. Proc. Natl. Acad. Sci. USA 100, 5063.
      Ikehara, Y., et al. 1994. Methods. Enzymol. 244, 215.
      David, F., et al. 1993. J. Biol. Chem. 268, 17247.
      Thomsen, P.D., et al. 1993. Mamm. Genome 4, 604.
      Misumi, Y., et al. 1992. Biochim. Biophys. Acta. 1131, 333.
      Seidl, R., et al. 1991. Biol. Chem. Hoppe Seyler 372, 213.
      Checler, F., et al. 1985. J. Neurochem. 45, 1509.
      Imai, K., et al. 1983. J. Biochem. 93, 431.
      Kato, T., et al. 1979. Experientia. 35, 409.
      Kojima, K., et al. 1979. Anal. Biochem. 100, 43.
      Kato, T., et al. 1978. Biochem. Med. 19, 351.
      Kenny, A.J., et al. 1976. Biochem. J. 157, 169.