The presence of glutaminase activity, or any other non-specific enzymatic activity, is not assayed for this product.
A3809
Asparaginase from Escherichia coli
lyophilized powder, 100-300 units/mg protein (biuret)
Sinónimos:
L-Asparagine Amidohydrolase
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Formulario
lyophilized powder
Nivel de calidad
actividad específica
100-300 units/mg protein (biuret)
composición
Protein, ≥60%
temp. de almacenamiento
2-8°C
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Aplicación
Acciones bioquímicas o fisiológicas
Asparaginase (ASNase) products are usually obtained from Escherichia coli and Erwinia chrysanthemi. These enzymes can block the synthesis of protein in tumor cells. It shows high activity in the G1 phase of the cell cycle.[6] It is capable of causing pancreatitis in leukemia patients.[2]
Asparaginase is used in enzymatic assays and to convert asparagine to aspartic acid. Asparaginase is used to reduce the formation of acrylamide in starchy food products. It is also used as a chemotherapy agent for acute lymphoblastic leukemia [7]. Product A3809 is from Escherichia coli and is provided as a lyophilized powder containing sodium chloride.
Definición de unidad
One unit will liberate 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 at 37 °C.
Forma física
Lyophilized powder containing sodium chloride
Nota de preparación
Chromatographically purified
Nota de análisis
Protein determined by biuret.
Palabra de señalización
Warning
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Repr. 2 - Skin Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges
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Certificados de análisis (COA)
Lot/Batch Number
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Jie Xiong et al.
EBioMedicine, 72, 103614-103614 (2021-10-11)
Metabolic reprogramming plays an essential role on lymphoma progression. Dysregulation of glutamine metabolism is implicated in natural-killer T-cell lymphoma (NKTCL) and tumor cell response to asparaginase-based anti-metabolic treatment. To understand the metabolomic alterations and determine the potential therapeutic target of
Asparagine Synthetase Is Highly Expressed at Baseline in the Pancreas Through Heightened PERK Signaling
Mukherjee A, et al.
Cellular and molecular gastroenterology and hepatology (2019)
Oxidized phospholipids regulate amino acid metabolism through MTHFD2 to facilitate nucleotide release in endothelial cells
Hitzel J, et al.
Nature Communications, 9(2292), 1-18 (2018)
Purification, characterization and immunogenicity assessment of glutaminase free L-asparaginase from Streptomyces brollosae NEAE-115
El-Naggar NEA, et al.
BMC Pharmacology & Toxicology, 19(1), 1-15 (2018)
Changes in plasma angiotensin subtypes in Japanese eel acclimated to various salinities from deionized water to double-strength seawater
Wong MKS, et al.
General and Comparative Endocrinology, 178(2), 250-258 (2012)
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Is there any Glutaminase activity of Product No. A3809?
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I would like to know the amino acid sequence of this enzyme (Product No. A3809) and the strain of E. coli from which this enzyme is derived.
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This enzyme is obtained from a natural extraction of E. coli. It is not from a recombinant source. The strain of E. coli used is considered proprietary.
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What is the actual quantity (in the gram) in 1 unite of the enzyme. Because, we want use the enzyme in gram. such as i have 300 unit of this enzyme. So please tell what is the exact quantity in gram
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The activity of this product varies from lot to lot with the minimum amount in a 1000 unit vial being 3.33 mg. This is based on the maximum allowable activity of 300 units per milligram protein and the maximum 100% protein. The maximum amount will be 16 mg per 1000 unit vial. This is based on the minimum allowable activity of 100 units per milligram protein and the minimum allowable protein content of 60%. Please see the link below to access a sample or lot specific Certificate of Analysis:
https://www.sigmaaldrich.com/product/sigma/a3809#product-documentationHelpful?
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I would like to obtain the asparaginase (A3809-1KU) enzymatic assay protocol.
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Please see the protocol at the link below:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/369/983/a3809enz.pdfHelpful?
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What is the molecular weight of this enzyme (Product No. A3809)?
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This enzyme consists of a tetramer composed of four identical subunits of 34,080 Daltons each. The molecular weight of the tetramer is 136,320 Daltons.
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What is the source of this enzyme (Product No. A3809)?
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This enzyme is obtained from a natural extraction of E. coli. It is not from a recombinant source.
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What is the Department of Transportation shipping information for this product?
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Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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How does the storage temperature relate to shipping conditions?
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The storage conditions that a Sigma-Aldrich catalog and label recommend for products are deliberately conservative. For many products, long-term storage at low temperatures will increase the time during which they are expected to remain in specification and therefore are labeled accordingly. Where short-term storage, shipping time frame, or exposure to conditions other than those recommended for long-term storage will not affect product quality, Sigma-Aldrich will ship at ambient temperature. The products sensitive to short-term exposure to conditions other than their recommended long-term storage are shipped on wet or dry ice. Ambient temperature shipping helps to control shipping costs for our customers. At any time, our customers can request wet- or dry-ice shipment, but the special handling is at customer expense if our product history indicates that the product is stable for regular shipment.
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How should this enzyme (Product No. A3809) be reconstituted?
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Prior to determining the activity of this enzyme, Sigma reconstitutes it directly in deionized water. Solutions should be prepared fresh, as the stability of stock solutions has not been evaluated.
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