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A3809

Sigma-Aldrich

Asparaginase from Escherichia coli

lyophilized powder, 100-300 units/mg protein (biuret)

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Synonym(s):
L-Asparagine Amidohydrolase
CAS Number:
9015-68-3
Enzyme Commission number:
3.5.1.1 (BRENDA, IUBMB)
EC Number:
232-765-3
MDL number:
MFCD00130565
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

200

specific activity

100-300 units/mg protein (biuret)

composition

Protein, ≥60%

storage temp.

2-8°C

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General description

Asparaginase is a bacterial enzyme and also a chemotherapeutic drug.

Application

Asparaginase from Escherichia coli has been used:
  • to compare the cytotoxic effect of L-asparaginase purified from Streptomyces brollosae NEAE-115
  • as a standard in asparaginase assay to quantify asparaginase activities in various eel tissues
  • to elicit amino acid deprivation

Biochem/physiol Actions

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. It is capable of causing pancreatitis in leukemia patients.
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 . Product A3809 is from Escherichia coli and is provided as a lyophilized powder containing sodium chloride.
Asparaginase may cause cell death in leukemic cells by converting the necessary L-asparagine to aspartic acid and ammonia . Asparaginase is allosterically regulated and is crucial for proper cell functioning .

Unit Definition

One unit will liberate 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 at 37 °C.

Physical form

Lyophilized powder containing sodium chloride

Preparation Note

Chromatographically purified

Analysis Note

Protein determined by biuret.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Warning

Hazard Statements

H317,H361

Hazard Classifications

Repr. 2 - Skin Sens. 1

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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  1. How does the storage temperature relate to shipping conditions?

    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. See Shipping and Storage for more information.

  2. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  3. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  4. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  5. What is the Department of Transportation shipping information for this product?

    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. 

  6. How should this enzyme (Product No. A3809) be reconstituted?

    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.

  7. What is the source of this enzyme (Product No. A3809)?

    This enzyme is obtained from a natural extraction of E. coli. It is not from a recombinant source.

  8. What is the molecular weight of this enzyme (Product No. A3809)?

    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.

  9. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

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)
L-Asparaginase: discovery and development as a tumor-inhibitory agent.
J D Broome
Cancer treatment reports, 65 Suppl 4, 111-114 (1981-01-01)
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