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317639 Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda

317639
Purchase on Sigma-Aldrich

Descripción

Replacement Information

Products

Número de referenciaEmbalaje Cant./Env.
317639-5MIU Ampolla de plást. 5 miu
Description
OverviewRecombinant, human DPP IV fused at the N-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells. A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. Note: 1 mU = 1 milliunit.
Note: 1 mU = 1 milliunit.
Catalogue Number317639
Brand Family Calbiochem®
SynonymsCD26, DPPIV
References
ReferencesPospisilik, JA, et al. 2003. Diabetes 52, 741.
Dobers, J., et al. 2002. Protein Expr. Purif. 25, 527.
Marguet, D., et al. 2000. Proc. Natl. Acad. Sci. 97, 6874.
Misumi, Y., et al. 1992. Biochim. Biophys. Acta 1131, 333.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmole H-Gly-Pro-AMC per min at 37°C, pH 8.0.
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≥8 U/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 InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Número de referencia GTIN
317639-5MIU 04055977216240

Documentation

Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda Ficha datos de seguridad (MSDS)

Título

Ficha técnica de seguridad del material (MSDS) 

Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda Certificados de análisis

CargoNúmero de lote
317639

Referencias bibliográficas

Visión general referencias
Pospisilik, JA, et al. 2003. Diabetes 52, 741.
Dobers, J., et al. 2002. Protein Expr. Purif. 25, 527.
Marguet, D., et al. 2000. Proc. Natl. Acad. Sci. 97, 6874.
Misumi, Y., et al. 1992. Biochim. Biophys. Acta 1131, 333.
Ficha técnica

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.

Revision17-May-2010 JSW
SynonymsCD26, DPPIV
DescriptionRecombinant, human DPP IV fused at the N-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells. A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. Note: 1 mU = 1 milliunit.
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
EC number3.4.14.5
Purity≥90% by SDS-PAGE
Specific activity≥8 U/mg protein
Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmole H-Gly-Pro-AMC per min at 37°C, pH 8.0.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesPospisilik, JA, et al. 2003. Diabetes 52, 741.
Dobers, J., et al. 2002. Protein Expr. Purif. 25, 527.
Marguet, D., et al. 2000. Proc. Natl. Acad. Sci. 97, 6874.
Misumi, Y., et al. 1992. Biochim. Biophys. Acta 1131, 333.