Analytical Data
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Gene name
IpaD
- Application
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Alternative Names
IpaD；Invasin IpaD
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MNITTLTNSISTSSFSPNNTNGSSTETVNSDIKTTTSSHPVSSLTMLNDT LHNIRTTNQALKKELSQKTLTKTSLEEIALHSSQISMDVNKSAQLLDILS RNEYPINKDARELLHSAPKEAELDGDQMISHRELWAKIANSINDINEQYL KVYEHAVSSYTQMYQDFSAVLSSLAGWISPGGNDGNSVKLQVNSLKKALE ELKEKYKDKPLYPANNTVSQEQANKWLTELGGTIGKVSQKNGGYVVSINM TPIDNMLKSLDNLGGNGEVVLDNAKYQAWNAGFSAEDETMKNNLQTLVQK YSNANSIFDNLVKVLSSTISSCTDTDKLFLHF
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Molecular Weight
57 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 (Invasion Plasmid Antigen D) is a critical virulence factor secreted by Shigella flexneri, a pathogenic bacterium responsible for shigellosis, a severe form of bacterial dysentery. IpaD plays a vital role in the invasion process of epithelial cells by facilitating the formation of membrane protrusions that allow bacterial entry. Researchers have focused on characterizing IpaD due to its potential as a target for vaccine development and therapeutic interventions against Shigella infections. The protein is involved in the modulation of host cell signaling, which aids in bacterial entry and survival within the host. Additionally, IpaD interacts with various host proteins, leading to the activation of inflammatory pathways, further exacerbating tissue damage. Recent studies have employed recombinant DNA technology to produce IpaD for structural and functional analyses, enabling the elucidation of its mechanism of action and interactions with host cells. Understanding IpaD's role in Shigella pathogenesis is crucial for developing strategies to combat infections, as the bacterium exhibits increasing resistance to conventional antibiotics. Thus, the research into IpaD recombinant proteins not only contributes to fundamental microbiology but also holds promise for innovative public health solutions against bacterial diseases like shigellosis.
