Analytical Data
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Gene name
IX
- Application
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Alternative Names
Coat protein C, polypeptide II G9P
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Species
Enterobacteria phage M13
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P69538
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Expression Region
1-32aa
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Molecular Weight
19.7 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 IX protein, a key component of the adenoviral structure, has garnered significant attention in the field of molecular biology and virology due to its crucial role in the assembly and stability of the viral capsid. This protein is encoded by the adenoviral genome, and its function has implications not only for understanding viral replication and pathogenesis but also for potential therapeutic applications. Research into IX protein has revealed its involvement in interacting with other viral proteins and host cell pathways, thus influencing the efficiency of viral infection and immune evasion. Additionally, IX protein is being explored as a target for vaccine development and gene delivery systems due to its immunogenic properties and ability to enhance the stability of viral vectors. Advances in techniques such as cryo-electron microscopy and X-ray crystallography have provided insights into the structural characteristics of the IX protein, paving the way for innovative strategies to manipulate adenoviral vectors for biotechnological and medical purposes. As the demand for effective gene therapy and vaccine platforms continues to rise, understanding the nature and functioning of the IX protein is crucial for harnessing adenoviral systems for safe and efficient applications in modern medicine.
