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437996 5-Lipoxygenase, Human, Recombinant, S. fruigiperda

437996
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Panoramica

Replacement Information

Products

Numero di catalogoConfezionamento Qtà/conf
437996-500U Fiala di plastica 500 u
Description
OverviewRecombinant, human 5-Lipoxygenase expressed in S. fruigiperda insect cells using a baculovirus overexpression system. 5-LO catalyzes the formation of 5(S)-HpETE from arachidonic acid and its subsequent conversion to leukotriene A4. It is localized in the cytosol of resting human and rat peripheral blood neutrophils, whereas it is found in the nucleus in rat basophilic leukemia cells and human alveolar macrophages. Upon stimulation of the cell, 5-LO translocates to the nuclear membrane where it is found in association with 5-LO activating protein (FLAP) and with the 85 kDa cPLA2.
Catalogue Number437996
Brand Family Calbiochem®
Synonyms5-LO
References
ReferencesBrock, T.G., et al. 1997. J. Biol. Chem. 272, 8276.
Pouliot, M., et al. 1996. Eur. J. Biochem. 238, 250.
Zhang, Y.Y., et al. 1993. J. Biol. Chem. 268, 2535.
Shimizu, T., et al. 1984. Proc. Natl. Acad. Sci. USA 81, 689.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that consumes 1.0 nmol of oxygen per min at 25°C in 50 mM Tris-HCl, 100 µM arachidonate, 2 mM CaCl₂, 1 mM ATP, 250 µM oxygen. Oxygen consumption can be measured using a oxygraph equipped with a Clark oxygen electrode.
EC number1.13.11.34
FormLiquid
FormulationIn 100 mM Tris containing 5 mM EGTA, pH 8.0.
Quality LevelMQ100
Applications
Biological Information
Specific Activity~20 units/mg
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
Numero di catalogo GTIN
437996-500U 04055977186901

Documentation

5-Lipoxygenase, Human, Recombinant, S. fruigiperda MSDS

Titolo

Scheda di sicurezza (MSDS) 

5-Lipoxygenase, Human, Recombinant, S. fruigiperda Certificati d'Analisi

TitoloNumero di lotto
437996

Riferimenti bibliografici

Panoramica delle referenze
Brock, T.G., et al. 1997. J. Biol. Chem. 272, 8276.
Pouliot, M., et al. 1996. Eur. J. Biochem. 238, 250.
Zhang, Y.Y., et al. 1993. J. Biol. Chem. 268, 2535.
Shimizu, T., et al. 1984. Proc. Natl. Acad. Sci. USA 81, 689.
Scheda tecnica

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.

Revision06-August-2008 RFH
Synonyms5-LO
DescriptionRecombinant, human 5-Lipoxygenase expressed in S. fruigiperda insect cells using a baculovirus overexpression system. It is localized in the cytosol of resting neutrophils, and is found in the nucleus in rat basophilic leukemia cells and human alveolar macrophages. Upon stimulation of the cell, 5-LO translocates to the nuclear membrane where it is found in association with 5-LO activating protein (FLAP) and with the 85 kDa cPLA2.
FormLiquid
FormulationIn 100 mM Tris containing 5 mM EGTA, pH 8.0.
EC number1.13.11.34
Specific activity~20 units/mg
Unit definitionOne unit is defined as the amount of enzyme that consumes 1.0 nmol of oxygen per min at 25°C in 50 mM Tris-HCl, 100 µM arachidonate, 2 mM CaCl₂, 1 mM ATP, 250 µM oxygen. Oxygen consumption can be measured using a oxygraph equipped with a Clark oxygen electrode.
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesBrock, T.G., et al. 1997. J. Biol. Chem. 272, 8276.
Pouliot, M., et al. 1996. Eur. J. Biochem. 238, 250.
Zhang, Y.Y., et al. 1993. J. Biol. Chem. 268, 2535.
Shimizu, T., et al. 1984. Proc. Natl. Acad. Sci. USA 81, 689.