Analytical Data
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Gene name
isdA
- Application
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Alternative Names
Fur-regulated protein A Staphylococcal transferrin-binding protein A frpA, stbA
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Species
Staphylococcus aureus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6GA85
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Expression Region
47-316aa
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Molecular Weight
35.1 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
Related Products
Protein Description
IsdA (Iron-regulated surface determinant A) is a significant component in the pathogenicity of certain bacterial strains, particularly Staphylococcus aureus. Understanding the structure and function of IsdA is crucial as it plays a pivotal role in iron acquisition, which is vital for bacterial survival and proliferation in the iron-limited environments of a host organism. Research has shown that IsdA interacts with hemoglobin, facilitating the extraction of heme, an iron-containing compound that bacteria utilize for their metabolic processes. This mechanism underscores the importance of IsdA not only in the context of bacterial virulence but also as a potential target for novel therapeutic strategies aimed at combatting infections. The study of IsdA is further accentuated by the increasing prevalence of antibiotic-resistant strains of S. aureus, prompting the need for alternative approaches to treatment. Recombinant IsdA proteins have been generated for detailed structural studies and functional assays, allowing researchers to explore the molecular mechanisms underlying heme uptake. These studies offer insights into the interaction of IsdA with host proteins and the potential for developing vaccines or inhibitors based on its structure. As such, ongoing research into IsdA and its recombinant forms represents a vital intersection of microbiology, biochemistry, and medical research, promising to advance our understanding of bacterial pathogenesis and lead to innovative solutions in infectious disease management.
