ANTIBODIES

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Anti-Sea Louse

Cat. #158066

Tool name: Anti-Sea Louse
Tool type: Antibodies
Class: Polyclonal
Conjugate: Unconjugated
Reactivity: Sea Louse
Host: Rabbit
Molecular weight of the target: 41
Application: ELISA
Description: The salmon louse (Lepeophtheirus salmonis) is an ectoparasitic copepod with a complex life cycle. It feeds on the mucus, skin and blood of salmonid fish species, causes significant losses in salmon aquaculture. The parasite can persist on the surface of the fish without any effective control being exerted by the host immune system. Given the challenges with currently available methods, vaccination appears as an attractive, environmentally sound strategy. The challenge of developing vaccines against ectoparasites arises from the need to understand the complex molecular interactions between vertebrate hosts and ectoparasites, which require the discovery of key pathway molecules that mediate ectoparasite-host interactions. Calreticulin released by an intracellular parasite is capable of entering the cytoplasm, which is able to be processed via MHC class I. It could compete with host calreticulin for the binding of MHC molecules, and thus interfere with peptide loading and presentation. This is a valuable tool to monitor Calreticulin's role in parasite development as well as immune modulation of the host.
Immunogen: Ovalbumin-conjugated synthetic peptide.
Research area: Cell biology; Immunology

Target: Sea Louse (Lepeophtheirus salmonis) antigen (calreticulin)
Target molecular weight: 41
Target background: The salmon louse (Lepeophtheirus salmonis) is an ectoparasitic copepod with a complex life cycle. It feeds on the mucus, skin and blood of salmonid fish species, causes significant losses in salmon aquaculture. The parasite can persist on the surface of the fish without any effective control being exerted by the host immune system. Given the challenges with currently available methods, vaccination appears as an attractive, environmentally sound strategy. The challenge of developing vaccines against ectoparasites arises from the need to understand the complex molecular interactions between vertebrate hosts and ectoparasites, which require the discovery of key pathway molecules that mediate ectoparasite-host interactions. Calreticulin released by an intracellular parasite is capable of entering the cytoplasm, which is able to be processed via MHC class I. It could compete with host calreticulin for the binding of MHC molecules, and thus interfere with peptide loading and presentation. This is a valuable tool to monitor Calreticulin's role in parasite development as well as immune modulation of the host.

£ 300
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