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Molecular Depot Basic PLA2 homolog MjTX-I (Bothrops moojeni) B2016746

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    Purchase Molecular Depot Basic PLA2 homolog MjTX-I (Bothrops moojeni) B2016746

    Molecular Depot Basic PLA2 homolog MjTX-I (Bothrops moojeni) B2016746

    SKU: b2016746


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    Vendor: molecular depot
    Shipping Weight: 1.00 pounds
    Part Number: molecular-depot-b2016746
    Our Price:
    $695.00 $1,395.00
    Sale Savings: $700.00

    Molecular Depot Basic PLA2 homolog MjTX-I (Bothrops moojeni) B2016746

    Basic PLA2 homolog MjTX-I (Bothrops moojeni) is a high quality protein found in the venom of the snake Bothrops moojeni. It is a phospholipase A2 enzyme, which is an important component of snake venom that plays a role in the toxicity of the venom by disrupting cell membranes and causing tissue damage. MjTX-I is a basic form of phospholipase A2, meaning it has a higher pH optimum for activity compared to acidic forms. It is important for the snake’s ability to immobilize and digest its prey. 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.

    Basic PLA2 homolog MjTX-I (Bothrops moojeni)
    Catalog number:B2016746
    Lot number:Batch Dependent
    Expiration Date:Batch dependent
    Amount:25 µg
    Molecular Weight or Concentration:13.8 kDa
    Supplied as:Solution
    Applications:a molecular tool for various biochemical applications
    Storage:-80°C
    Keywords:Basic Phospholipase A2 homolog 1, Basic PLA2 homolog BomoTx, B. moojeni Myotoxin I, svPLA2 homolog
    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:
    1: Saito K. Reminiscence of phospholipase B in Penicillium notatum Proc Jpn Acad Ser B Phys Biol Sci. 2014;90(9):333-46.
    2: Scott KF, Mann TJ, Fatima S, Sajinovic M, Razdan A, Kim RR, Cooper A, Roohullah A, Bryant KJ, Gamage KK, Harman DG, Vafaee F, Graham GG, Church WB, Russell PJ, Dong Q, de Souza P. Human Group IIA Phospholipase A(2)-Three Decades on from Its Discovery Molecules. 2021 Nov 30;26(23):7267.
    3: Patel YC, Greenwood MT, Panetta R, Demchyshyn L, Niznik H, Srikant CB. The somatostatin receptor family Life Sci. 1995;57(13):1249-65.
    4: Vadas P, Browning J, Edelson J, Pruzanski W. Extracellular phospholipase A2 expression and inflammation: the relationship with associated disease states J Lipid Mediat. 1993 Aug;8(1):1-30.
    5: Campos PC, de Melo LA, Dias GLF, Fortes-Dias CL. Endogenous phospholipase A(2) inhibitors in snakes: a brief overview J Venom Anim Toxins Incl Trop Dis. 2016 Dec 21;22:37.
    6: Bickler PE. Amplification of Snake Venom Toxicity by Endogenous Signaling Pathways Toxins (Basel). 2020 Jan 22;12(2):68.
    7: Yaginuma S, Kawana H, Aoki J. Current Knowledge on Mammalian Phospholipase A(1), Brief History, Structures, Biochemical and Pathophysiological Roles Molecules. 2022 Apr 12;27(8):2487.
    8: Castro-Amorim J, Novo de Oliveira A, Da Silva SL, Soares AM, Mukherjee AK, Ramos MJ, Fernandes PA. Catalytically Active Snake Venom PLA(2) Enzymes: An Overview of Its Elusive Mechanisms of Reaction J Med Chem. 2023 Apr 27;66(8):5364-5376.
    9: Vorotnikov AV, Tyurin-Kuzmin PA. Chemotactic signaling in mesenchymal cells compared to amoeboid cells Genes Dis. 2014 Sep 28;1(2):162-173.
    10: Ma X, Liu H, Liu Z, Wang Y, Zhong Z, Peng G, Gu Y. Trichosporon asahii PLA2 Gene Enhances Drug Resistance to Azoles by Improving Drug Efflux and Biofilm Formation Int J Mol Sci. 2023 May 16;24(10):8855.

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