Analytical Data
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Gene name
IpaD
- Application
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Alternative Names
36KDA membrane antigen
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Species
Shigella flexneri
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18013
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Expression Region
1-332aa
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Molecular Weight
56.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
IpaD is an essential protein derived from the intracellular bacterium Shigella flexneri, which is a significant causative agent of bacterial dysentery in humans. Research surrounding IpaD has gained prominence due to its critical role in the type III secretion system (T3SS), a sophisticated molecular syringe utilized by Shigella to inject effector proteins into host cells, facilitating bacterial invasion and immune evasion. Understanding the structure and function of IpaD is vital, as it acts as a key regulator in T3SS assembly and effector translocation. The protein has garnered attention for its potential as a vaccine candidate and for its utility in developing novel therapeutic strategies against Shigella infections. Studies have revealed that IpaD interacts with various host cell components, contributing to the pathogenicity of Shigella. Furthermore, the exploration of IpaD re-combinantly expressed in different systems offers insights into its immunogenic properties and biological functionalities. This research could pave the way for innovative interventions that target the T3SS, ultimately leading to enhanced prevention and treatment options for shigellosis and related diseases. As antibiotic resistance continues to rise, the significance of non-antibiotic therapeutics derived from an understanding of IpaD and its mechanisms becomes increasingly critical.
