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Scorpion toxin bound to antibody C015 / 5158

Scorpion toxin bound to antibody C015  /  5158


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Scorpion toxin bound to antibody C015 / 5158

Scorpion toxin bound to antibody, molecular model. The toxin is Cn2 from a Centruroides noxius scorpion. The antibodies are human single-chain antibody fragments (scFv) called 9004G. The antibodies, forming part of the human immune system, have the effect of neutralising the scorpion toxin

Science Photo Library features Science and Medical images including photos and illustrations

Media ID 9208605

© LAGUNA DESIGN/SCIENCE PHOTO LIBRARY

Antibodies Antibody Arachnid Arthropod Biomolecule Graphic Immunological Immunology Macromolecule Molecular Biology Molecules Poison Proteins Proteomics Scorpion Structural Toxic Toxin Venom Biochemical Biochemistry Cutouts Molecular Model Molecular Structure Protein


EDITORS COMMENTS
This print showcases the intricate molecular structure of scorpion toxin bound to antibody C015/5158. Against a striking black background, this illustration highlights the venomous nature of these arthropods and their potent biochemical capabilities. The scorpion toxin, known as Cn2 from Centruroides noxius species, is depicted in vibrant detail, revealing its toxic properties. The antibodies featured in this image are human single-chain antibody fragments (scFv) called 9004G. These remarkable molecules play a crucial role in our immune system by neutralizing the harmful effects of scorpion toxins. Their presence signifies the power of our biological defense mechanisms against such threats. With precision and artistry, Laguna Design has created an extraordinary visual representation that merges biology and graphic design seamlessly. This molecular model provides valuable insights into the structural composition of both the toxin and antibodies at a microscopic level. Immunology enthusiasts and researchers alike will appreciate this stunning artwork for its scientific accuracy and aesthetic appeal. It serves as a testament to the wonders of molecular biology and proteomics while reminding us of nature's ability to produce both beauty and danger within its smallest building blocks.

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