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317640 Dipeptidyl Peptidase IV (CD26), Porcine Kidney

FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.

Synonymes: CD26, DPPIV

317640
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Aperçu

Replacement Information

Products

RéférenceConditionnement Qté
317640-250MIU Ampoule plast. 250 miu
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
Global Trade Item Number
Référence GTIN
317640-250MIU 04055977216257

Documentation

Dipeptidyl Peptidase IV (CD26), Porcine Kidney FDS

Titre

Fiche de données de sécurité des matériaux (FDS) 

Dipeptidyl Peptidase IV (CD26), Porcine Kidney Certificats d'analyse

TitreNuméro de lot
317640

Références bibliographiques

Aperçu de la référence bibliographique
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.
Fiche technique

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 Avoid freeze/thaw
≤ -70°C
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.