317640 Dipeptidyl Peptidase IV (CD26), Porcine Kidney

317640
Cenu nelze zjistit
Minimum Quantity needs to be mulitiple of
S dokončenou objednávkou Další informace
Ušetřili jste ()
 
Vyžádat nacenění
Omezená dostupnostOmezená dostupnost
Na skladě 
Přerušeno
Dostupné omezené množství
Dostupnost bude potvrzena
    Remaining : Will advise
      Remaining : Will advise
      Bude poskytnuto
      Kontaktujte Zákaznický servis
      Contact Customer Service
      Zobrazit ceny a dostupnost

      Přehled

      Replacement Information

      Tabulka spec. kláve

      Ceny a dostupnost

      Katalogové číslo DostupnostBalení ks/bal. Cena Množství
      317640-250MIU
      Zjišťuji dostupnost...
      Omezená dostupnostOmezená dostupnost
      Na skladě 
      Přerušeno
      Dostupné omezené množství
      Dostupnost bude potvrzena
        Remaining : Will advise
          Remaining : Will advise
          Bude poskytnuto
          Kontaktujte Zákaznický servis
          Contact Customer Service

          Plastová ampulka 250 miu
          Zjišťuji cenu...
          Cenu nelze zjistit
          Minimum Quantity needs to be mulitiple of
          S dokončenou objednávkou Další informace
          Ušetřili jste ()
           
          Vyžádat nacenění
          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 MSDS

          Title

          Safety Data Sheet (SDS) 

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

          TitleLot Number
          317640

          References

          Přehled odkazů
          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.