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  • Size:
    12 species, 2D HPLC, 1mg protein/fraction
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      • Overview
        • Venoms are a proven therapeutic resource with several drugs on the market in cardiovascular biology such as anticoagulants and antihypertensives. Snake venoms are a rich source of new cardiovascular tools such as C-type lectins, serine proteases, natriuretics and a wealth of signalling peptides. These targeted arrays contain pure venom fractions from 12, 24, 48 or 96 species optimised for identification of novel tools. Each array contains characterised venoms active in analgesic pathways from the literature to act as positive controls. The control venoms for T-VDACV include Crotalus adamanteus (eastern diamondback rattlesnake) where several bradykinin potentiating peptides have been discovered [1]; Dendroaspis angusticeps (eastern green mamba) where several novel natriuretic peptides have been discovered [2]; and Bitis gabonica (Gaboon viper) venom which contains a large abundance of serine proteases and, in particular, rhinocerase [3]. Other venom fractions making up the library have been specially selected by our drug discovery scientists to maximise novel hit potential.
          • Venoms are supplied lyophilised in Echo qualified acoustic source plates (Labcyte Inc) and are useable on any SBS footprint liquid handling device or by hand.
          • 384-well format has 200ng venom fraction per well, suggested dilution 20µl as hit fractions are typically active at 5µg/ml and below.
          • 1536-well format also available.

          Please contact us at  for specific academic pricing.


          1. Wermelinger L.S., Dutra D.L., Oliveira-Carvalho A.L., Soares M.R., Bloch C. Jr., Zingali R.B. (2005). Fast analysis of low molecular mass compounds present in snake venom: identification of ten new pyroglutamate- containing peptides. Rapid Commun. Mass Spectrom. 19:1703-1708
          2. Vink S, Jin A.H., Poth K.J., Head G.A., Alewood P.F., (2012). Natriuretic peptide drug leads from snake venom. Toxicon. Mar 15;59(4).
          3. Vaiyapuri S., Harrison R.A., Bicknell A.B., Gibbins J.M., Hutchinson G. (2010). Purification and functional characterisation of rhinocerase, a novel serine protease from the venom of Bitis gabonica rhinoceros. PLoS ONE 5:E9687-E9687

      • Properties
        • Storage
          Recommend storage at -20°C upon receipt. Lyophilised T-VDAs™ are shipped at ambient temperature, as they are stable for several weeks.
          Research Field
          Cardiovascular – coagulation, blood pressure, haemorrhage
      • Applications
        • Application Description
           T-VDAs™ can be used in any biochemical or cell based assay like any other compound array. The fractionated T-VDAs perform well in Phenotypic assays.
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