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MilliporeSigma

A3809

Asparaginase from Escherichia coli

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

Synonym(s):

L-Asparagine Amidohydrolase

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100 UNITS

$426.00

1000 UNITS

$2,010.00

$426.00


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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-765-3
MDL number:
EC Number:

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Product Name

Asparaginase from Escherichia coli, lyophilized powder, 100-300 units/mg protein (biuret)

form

lyophilized powder

specific activity

100-300 units/mg protein (biuret)

composition

Protein, ≥60%

storage temp.

2-8°C

Quality Level

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This Item
A6007G5635A7437
specific activity

100-300 units/mg protein (biuret)

specific activity

75-150 units/mg solid

specific activity

≥500 units/mg protein

specific activity

≥150 units/mg protein (biuret)

form

lyophilized powder

form

soluble powder

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

300

Quality Level

200

composition

Protein, ≥60%

composition

-

composition

Protein, ≥60% biuret

composition

Protein, 5.0-20.0%

Analysis Note

Protein determined by biuret.

Application

Asparaginase from Escherichia coli has been used:
  • to compare the cytotoxic effect of L-asparaginase purified from Streptomyces brollosae NEAE-115[1]
  • as a standard in asparaginase assay to quantify asparaginase activities in various eel tissues[2]
  • to elicit amino acid deprivation[3]

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.[4] It is capable of causing pancreatitis in leukemia patients.[5]
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 [6]. 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 [6]. Asparaginase is allosterically regulated and is crucial for proper cell functioning [7].

General description

Asparaginase is a bacterial enzyme[8] and also a chemotherapeutic drug.[5]

Other Notes

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

pictograms

Health hazardExclamation mark

signalword

Warning

hcodes

Hazard Classifications

Repr. 2 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges


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Certificates of Analysis (COA)

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L-Asparaginase: discovery and development as a tumor-inhibitory agent.
J D Broome
Cancer treatment reports, 65 Suppl 4, 111-114 (1981-01-01)
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)
Antineoplastic Drugs
Pharmacology and Therapeutics for Dentistry, 530-562 (2017)
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)
Gabriel Álvares Borges et al.
Clinical and experimental pharmacology & physiology, 47(5), 857-866 (2020-01-17)
Asparaginase is fundamental to the treatment of haematological malignancies. However, little has been studied on the effects that asparaginase could exert on solid tumours. Thus, this study aimed to evaluate the effects of asparaginase on an oral carcinoma cell line.

Questions

1–9 of 9 Questions  
  1. Is there any Glutaminase activity of Product No. A3809?

    1 answer
    1. The presence of glutaminase activity, or any other non-specific enzymatic activity, is not assayed for this product.

      Helpful?

  2. 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.

    1 answer
    1. 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.

      Helpful?

  3. 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

    1 answer
    1. 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-documentation

      Helpful?

  4. I would like to obtain the asparaginase (A3809-1KU) enzymatic assay protocol.

    1 answer
    1. Helpful?

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

    1 answer
    1. 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.

      Helpful?

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

    1 answer
    1. 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.

      Helpful?

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

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

      Helpful?

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

    1 answer
    1. 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.

      Helpful?

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

    1 answer
    1. 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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