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Phospholipase A1 from Aspergillus oryzae Proteins Molecular Depot
Phospholipase A1 from Aspergillus oryzae Proteins Molecular Depot
Phospholipase A1 from Aspergillus oryzae Proteins Molecular Depot
Phospholipase A1 from Aspergillus oryzae Proteins Molecular Depot

Phospholipase A1 from Aspergillus oryzae

$1,395.00

    Catalog Number: B2017895 (25 mL)

    Phospholipase A1 from Aspergillus oryzae is an enzyme that belongs to the phospholipase A1 family. This enzyme specifically catalyzes the hydrolysis of the sn-1 acyl chain of phospholipids, resulting in the release of a free fatty acid and a lysophospholipid. Phospholipase A1 enzymes play important roles in lipid metabolism. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

    Products are for in vitro research use only (RUO).

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What's Included

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VR Headset

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2 Touch Controllers

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Charging Cable

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Power Adapter

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Glasses Spacer

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Phospholipase A1 from Aspergillus oryzae

Catalog number: B2017895
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 25 mL
Molecular Weight or Concentration: N/A
Supplied as: Solution
Applications: a molecular tool for various biochemical applications
Storage: 2-8°C
Keywords: Lecitase™ Ultra, PLA1
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References

  • EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP); Lambré C, Barat Baviera JM, Bolognesi C, Cocconcelli PS, Crebelli R, Gott DM, Grob K, Lampi E, Mengelers M, Mortensen A, Rivière G, Steffensen IL, Tlustos C, Van Loveren H, Vernis L, Zorn H, Andryszkiewicz M, di Piazza G, Kovalkovicova N, Liu Y, Chesson A. Safety evaluation of the food enzyme phospholipase A1 from the genetically modified Aspergillus oryzae strain NZYM-LJ EFSA J. 2022 Jul 6;20(7):e07381.
  • EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP); Lambré C, Barat Baviera JM, Bolognesi C, Cocconcelli PS, Crebelli R, Gott DM, Grob K, Lampi E, Mengelers M, Mortensen A, Rivière G, Steffensen IL, Tlustos C, Van Loveren H, Vernis L, Zorn H, Glandorf B, Roos Y, Liu Y, Lunardi S, Chesson A. Safety evaluation of the food enzyme phospholipase A1 from the genetically modified Aspergillus oryzae strain NZYM-PP EFSA J. 2023 Feb 26;21(2):e07835.
  • Shiba Y, Ono C, Fukui F, Watanabe I, Serizawa N, Gomi K, Yoshikawa H. High-level secretory production of phospholipase A1 by Saccharomyces cerevisiae and Aspergillus oryzae Biosci Biotechnol Biochem. 2001 Jan;65(1):94-101.
  • Watanabe I, Koishi R, Yao Y, Tsuji T, Serizawa N. Molecular cloning and expression of the gene encoding a phospholipase A1 from Aspergillus oryzae Biosci Biotechnol Biochem. 1999 May;63(5):820-6.
  • Mawatari S, Yunoki K, Sugiyama M, Fujino T. Simultaneous preparation of purified plasmalogens and sphingomyelin in human erythrocytes with phospholipase A1 from Aspergillus orizae Biosci Biotechnol Biochem. 2009 Dec;73(12):2621-5.
  • Joint FAO/WHO Expert Committee on Food Additives. Evaluation of certain food additives World Health Organ Tech Rep Ser. 2006;934:1-145, back cover.
  • Nakagawara C, Arioka M. Distinct enzymatic and cellular characteristics of two phospholipases A(1) in Aspergillus oryzae Biochem Biophys Res Commun. 2019 Oct 22;518(4):644-650.
  • Joint FAO/WHO Expert Committee on Food Additives; Bend J, Bolger M, Knaap AG, Kuznesof PM, Larsen JC, Mattia A, Meylan I, Pitt JI, Resnik S, Schlatter J, Vavasour E, Rao MV, Verger P, Walker R, Wallin H, Whitehouse B, Abbott PJ, Adegoke G, Baan R, Baines J, Barlow S, Benford D, Bruno A, Charrondiere R, Chen J, Choi M, DiNovi M, Fisher CE, Iseki N, Kawamura Y, Konishi Y, Lawrie S, Leblanc JC, Leclercq C, Lee HM, Moy G, Munro IC, Nishikawa A, Olempska-Beer Z, de Peuter G, Pronk ME, Renwick AG, Sheffer M, Sipes IG, Tritscher A, Soares LV, Wennberg A, Williams GM. Evaluation of certain food additives and contaminants World Health Organ Tech Rep Ser. 2007;(947):1-225, back cover.
  • Perczyk P, Gawlak R, Broniatowski M. Interactions of fungal phospholipase Lecitase ultra with phospholipid Langmuir monolayers – Search for substrate specificity and structural factors affecting the activity of the enzyme Biochim Biophys Acta Biomembr. 2021 Oct 1;1863(10):183687.

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Product Resources:

Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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