IAV-NP

Recombinant Influenza A Virus Nucleoprotein produced in E. coli having a Mw of 66.6kDa. IAV-NP is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

E. coli.

Sterile Filtered clear solution.

IAV-NP protein solution contains 0.25% sodium azide, 10mM K2CO3 and PBS.

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

Avoid multiple freeze-thaw cycles.

Protein is >90% pure as determined by 10% PAGE (coomassie staining).      

MASQGTKRSYEQMETDGERQNATEIRASVGKMIDGIGRFYIQMCTELKLSDYEGR LIQNSLTIERMVLSAFDERRNRYLEEHPSAGKDPKKTGGPIYKRVDGKWMRELVL YDKEEIRRIWR QANNGDDATRGLTHMMIWHSNLNDTTYQRTRALVRTGMDPRMC SLMQGSTLPRRSGAAGAAVKGIGTMVMELIRMIKRGINDRNFWRGENGRKTRSAY ERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFSARSALILRGSVAHKS CLPACVYGPAVSSGYDFEKEGYSLVGIDPFKLLQNSQVYSLIRPNENPAHKSQLVWM ACHSAAFEDLRLLSFIRGTKVCPRGKLSTRGVQIASNENMDNMESSTLELRSRYWAIR TRSGGNTNQQRASAGQISVQPTFSVQRNLPFEKSTVMAAFTGNTEGRTSDMRAEIIRMM

SDS

Influenza A virus, notorious for its ability to cause seasonal epidemics and occasional pandemics, poses a significant threat to global public health. The pursuit of effective countermeasures has led to the exploration of Influenza A Virus Nucleoprotein Recombinant as a key molecular protagonist in our defense against this elusive virus. This research endeavors to unravel the intricacies of the Nucleoprotein Recombinant, shedding light on its structural features, immunogenic prowess, and applications in vaccine development and antiviral therapies. By dissecting the properties of the Nucleoprotein Recombinant, scientists aim to fortify our defenses against Influenza A, potentially paving the way for a new era in influenza prevention and control.

Structural Insights into Nucleoprotein Recombinant:

The Influenza A Virus Nucleoprotein Recombinant, engineered to mirror crucial viral components, serves as a versatile tool for studying the virus's genetic material. A nuanced understanding of its three-dimensional structure and conformational intricacies is pivotal, not only for deciphering the virus's replication mechanisms but also for designing targeted interventions, such as vaccines and antiviral drugs.

Immunogenic Potential and Vaccine Development:

The quest for an effective influenza vaccine has been fueled by the virus's notorious mutability. Nucleoprotein Recombinant, designed to elicit strong immune responses, stands as a promising candidate for vaccine development. By presenting conserved viral elements to the immune system, the recombinant protein aims to induce robust and lasting immunity, thwarting the influenza virus's ability to evade immune detection through antigenic drift.

Application in Antiviral Therapies:

Beyond vaccination, Influenza A Virus Nucleoprotein Recombinant holds promise in the realm of antiviral therapies. The recombinant protein's ability to stimulate immune responses can be harnessed in the development of immunotherapies. Monoclonal antibodies derived from the Nucleoprotein Recombinant may offer targeted treatments, neutralizing the virus and potentially shortening the duration and severity of influenza infections.

Challenges and Future Directions:

While the Nucleoprotein Recombinant stands at the forefront of influenza research, challenges persist. The virus's ability to rapidly mutate demands ongoing vigilance and adaptability in recombinant strategies. Furthermore, considerations of vaccine safety, efficacy, and public acceptance necessitate continuous exploration to optimize the translational success of Nucleoprotein Recombinant-based interventions.

Influenza A Virus Nucleoprotein Recombinant emerges as a sentinel in the scientific arsenal against influenza, epitomizing the quest for innovative solutions in the face of viral challenges. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies position it as a pivotal player. As researchers continue to decipher the molecular intricacies of Nucleoprotein Recombinant, they not only fortify our defenses against influenza but potentially pave the way for a paradigm shift in our approach to influenza prevention and control, shaping the landscape of global health security.