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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Escherichia coli eltB/ltpB Protein, N-His-SUMO |
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Origin species | Escherichia coli |
Expression system | Prokaryotic expression |
Molecular weight | 24.04 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Ala22-Asn124 |
Aliases /Synonyms | Heat-labile enterotoxin B chain, LT-B, human, LTH-B, eltB, ltpB |
Reference | ARO-P11534 |
Note | For research use only. |
Recombinant Escherichia coli eltB/ltpB protein is a genetically engineered protein produced by the bacterium Escherichia coli. This protein is composed of two subunits, eltB and ltpB, which are derived from the heat-labile enterotoxin of E. coli. The recombinant protein has been extensively studied for its structure, activity, and potential applications in various fields.
The recombinant eltB/ltpB protein is a heterodimeric protein, consisting of two subunits, eltB and ltpB. Each subunit has a molecular weight of approximately 12 kDa. The eltB subunit contains the A and B domains, while the ltpB subunit contains the C and D domains. The A and C domains are responsible for the toxin activity, while the B and D domains are involved in receptor binding.
The structure of the recombinant protein is similar to that of the native heat-labile enterotoxin, with the A and C domains forming a ring-like structure and the B and D domains extending outwards. This structure allows the protein to interact with its target receptor and exert its biological activity.
The main activity of the recombinant eltB/ltpB protein is its ability to bind to the GM1 ganglioside receptor on the surface of intestinal epithelial cells. This binding triggers a signaling cascade that leads to the activation of adenylate cyclase and an increase in intracellular levels of cAMP. This, in turn, leads to the secretion of chloride ions and water into the intestinal lumen, resulting in diarrhea.
Apart from its enterotoxic activity, the recombinant protein has also been shown to have immunomodulatory effects. It can induce the production of pro-inflammatory cytokines and chemokines, as well as activate immune cells such as macrophages and dendritic cells. These properties make it a potential adjuvant for use in vaccines and immunotherapies.
The recombinant eltB/ltpB protein has a wide range of potential applications in various fields, including medicine, biotechnology, and food safety.
In medicine, the protein has been studied for its potential as a vaccine adjuvant. Its ability to activate the immune system and induce a strong immune response makes it a promising candidate for use in vaccines against bacterial and viral infections. It has also been investigated for its potential as a treatment for autoimmune diseases and cancer.
In biotechnology, the recombinant protein has been used as a tool for protein purification and as a fusion partner for the production of recombinant proteins. Its strong binding affinity to the GM1 receptor makes it a useful tool for studying receptor-ligand interactions.
In food safety, the recombinant eltB/ltpB protein has been studied for its potential as a diagnostic tool for detecting E. coli contamination in food. Its ability to specifically bind to the GM1 receptor makes it a sensitive and specific probe for the detection of E. coli.
Recombinant Escherichia coli eltB/ltpB protein is a genetically engineered protein with a heterodimeric structure and multiple biological activities. Its ability to bind to the GM1 receptor and activate the immune system makes it a promising candidate for use in vaccines, immunotherapies, and diagnostic tools. Further research and development of this protein could lead to new and innovative applications in various fields.
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