Analytical Data
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Gene name
ompA
- Application
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Alternative Names
ompA；ELA2；Neutrophil elastase
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Species
Human
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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
P45996
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Expression Region
22-359aa
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AA Sequence
APQENTFYAGVKAGQGSFHDGINNNGAIKKGLSSSNYGYRRNTFTYGVFG GYQILNQDNFGLAAELGYDDFGRAKLREAGKPKAKHTNHGAYLSLKGSYE VLDGLDVYGKAGVALVRSDYKFYEDANGTRDHKKGRHTARASGLFAVGAE YAVLPELAVRLEYQWLTRVGKYRPQDKPNTAINYNPWIGCINAGISYRFG QGEAPVVAAPEMVSKTFSLNSDVTFAFGKANLKPQAQATLDSVYGEISQV KSRKVAVAGYTNRIGSDAFNVKLSQERADSVANYFVAKGVAADAISATGY GEANPVTGATCDQVKGRKALIACLAPDRRVEIAVNGTK
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Molecular Weight
56 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
The ompA gene, encoding the outer membrane protein A (OmpA) of Escherichia coli, has garnered significant interest in microbiological and biotechnological research due to its vital roles in bacterial survival, virulence, and its potential applications in vaccine development and diagnostic tools. OmpA is known for its contribution to the structural integrity of the bacterial membrane, acting as a porin and facilitating the transport of small molecules. Moreover, it is implicated in bacterial adherence, invasion, and immune evasion, making it a crucial factor in the pathogenicity of E. coli. The recombinant expression of OmpA allows for the study of its functional properties and antigenic determinants, which is essential for understanding host-pathogen interactions. Recent advancements in genetic engineering and protein purification techniques have enabled researchers to produce and characterize OmpA in significant quantities, paving the way for its use as a candidate antigen in immunological assays and vaccine formulations. Additionally, the study of OmpA's interactions with host immune cells provides insights into the development of novel therapeutic strategies against E. coli infections. This multifaceted research surrounding OmpA highlights its importance not only in fundamental microbiology but also in practical applications concerning public health and disease prevention. By harnessing the potential of OmpA, scientists aim to contribute to the field of infectious diseases, ultimately enhancing our capacity to combat bacterial pathogens effectively.
