Abcam, ab243102, Anti-Heat-labile enterotoxin B chain antibody

Size: 200µg
Rabbit Polyclonal Heat-labile enterotoxin B chain antibody. Suitable for ELISA, Dot, WB and reacts with Clostridium perfringens, Purified native protein - Clostridium perfringens samples. Cited in 1 publication. Immunogen corresponding to Native Full Length Protein corresponding to Clostridium perfringens Heat-labile enterotoxin B chain.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Clostridium perfringens,
Applications:ELISA, Dot, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Native Full Length Protein corresponding to Clostridium perfringens Heat-labile enterotoxin B chain.P01558,
Specificity:Clostridium perfringens enterotoxin.(food-poisoning strains).

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 6.5 - 8.5Constituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Heat-labile enterotoxin B chain (LT-B) also known as Escherichia coli heat-labile enterotoxin subunit B plays an important role in the functioning of certain bacterial toxins. LT-B with a mass of approximately 11.6 kDa forms a pentameric structure. It expresses in specific strains of Escherichia coli often within the gastrointestinal tract. The B chain helps the toxin bind to host cells by interacting with the GM1 ganglioside receptors on the surface of epithelial cells facilitating the entry of the catalytic A subunit into the cell.
Biological function summary
LT-B acts as a non-toxic subunit that enables the binding of the toxin complex to target cells. It forms a pentamer a stable ring structure which contributes to the adherence of bacteria to intestinal mucosa. While LT-B itself is not toxic it is essential for the delivery of the toxic A chain which exerts the physiological effects of the toxin. The entire enterotoxin complex plays a part in increasing intestinal secretion resulting in symptoms such as diarrhea.
Pathways
LT-B facilitates the activation of signaling events in the host cell that lead to increased cyclic AMP levels via the adenylate cyclase pathway. This activation disrupts normal cellular ionic balances promoting fluid and electrolyte movement into the intestinal lumen. The pathways involving LT-B closely link to proteins such as GM1 ganglioside and adenylate cyclase coordinating to amplify the effects of the enterotoxin A subunit in signal transduction.
LT-B significantly contributes to conditions like traveler's diarrhea and other infections caused by enterotoxigenic Escherichia coli (ETEC). The B subunit's mediative properties of cell entry are important for these pathologies exacerbating the symptoms by enhancing toxin delivery and action. In the context of its involvement in disease the interaction with the A chain is fundamental as the A subunit's enzymatic activity results in the pathological hypersecretion observed in cases of ETEC infection.