Analytical Data
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Gene name
isaB
- Application
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Alternative Names
isaB;Immunodominant staphylococcal antigen B
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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
Q9LAB5
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Expression Region
37-175aa
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AA Sequence
AITPYYTYNGYIGNNANFILDKNFINAIKYDNVKFNGIKLAKTNTIKKVEKYDQTFKGVSAKGNEASQLQFVVKNNISLKDIQKAYGKDLKKENGKTKEADSGIFYYQNAKKTLGIWFVVDHNRVVEVTVGHTPYKTSK
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Molecular Weight
20.8 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
The study of IsaB recombinant protein is rooted in the growing interest in understanding the mechanisms of bacterial pathogenesis and the development of novel therapeutic strategies. IsaB, a protein associated with the pathogenicity of certain bacterial species, plays a crucial role in regulating iron homeostasis and facilitating the uptake of iron, an essential nutrient for bacterial survival and growth. The lack of effective treatments against antibiotic-resistant bacteria has heightened the urgency for new approaches, including the exploration of protein-based therapies. Research on IsaB is particularly significant due to its potential as a target for drug design, as inhibiting its function may disrupt bacterial iron acquisition, thereby attenuating virulence. Advances in recombinant DNA technology have enabled the production of IsaB in heterologous expression systems, allowing for detailed structural and functional studies. Understanding the three-dimensional structure of IsaB through techniques such as X-ray crystallography and cryo-electron microscopy can provide insights into its interaction with host factors and reveal potential binding sites for therapeutic agents. Furthermore, the characterization of IsaB's immunogenic properties may lead to the development of vaccine candidates against pathogenic bacteria. Overall, the exploration of IsaB recombinant protein is a vital endeavor in the field of microbiology, with implications for vaccine development, therapeutic interventions, and the mitigation of infectious diseases.











