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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| RCP1096-2 | 7 days | 2 µg | $120.00 |
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| RCP1096-10 | 7 days | 10 µg | $290.00 | |||
| RCP1096-1 | 7 days | 1 mg | $8,320.00 |
Product Overview | |
| Name | IBSP Human, HEK |
|---|---|
| Description | |
| Integrin Binding Sialoprotein Human Recombinant, HEK | |
| Source | |
| E. coli. | |
| Physical Appearance | |
| Sterile Filtered clear solution. | |
| Formulation | |
| IBV-NP protein solution contains 25mM K2CO3 and PBS. | |
| Stability | |
| 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. | |
| Amino acid sequence | |
| HMSNMDIDGMNTGTIDKTPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPDRTTTSSE DDVGRKAQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILL AATDDKKTEFQKKKNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIRITFLKEEVKT MYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTVPRRSGATGV AIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRN PGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATP VSILRMGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGA ALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADV KGNLLKMMNDSMAKKTSGNAFIGKKMFQISDKNKTNPIEIPIKQTIPNFFFGRDTAEDYDDLDYLE. | |
| Background | |
| Influenza B virus, often overshadowed by its influenza A counterpart, remains a substantial contributor to seasonal influenza infections and poses a considerable public health challenge. In the quest for effective countermeasures, Influenza B Virus Nucleoprotein Recombinant has emerged as a focal point in the ongoing battle against this resilient virus. This research endeavors to unveil the intricacies of the Nucleoprotein Recombinant, delving into its structural nuances, immunogenic capabilities, and applications in vaccine development and antiviral therapies. By dissecting the properties of the Nucleoprotein Recombinant, scientists aspire to fortify our defenses against Influenza B, potentially reshaping strategies for broader influenza immunity. Structural Insights into Nucleoprotein Recombinant: Engineered to replicate key viral components, the Influenza B Virus Nucleoprotein Recombinant serves as a molecular mirror, allowing a comprehensive study of the virus's genetic material. Understanding its three-dimensional structure and conformational intricacies is crucial, not only for decoding the virus's replication mechanisms but also for tailoring interventions like vaccines and antiviral drugs to specific vulnerabilities. Immunogenic Potential and Vaccine Development: The challenge of Influenza B's seasonal variability necessitates innovative approaches to vaccine development. Nucleoprotein Recombinant, designed to induce potent immune responses, emerges as a promising candidate. By presenting conserved viral elements to the immune system, the recombinant protein seeks to instigate robust and durable immunity, countering the virus's propensity for antigenic drift and promoting broader protection. Application in Antiviral Therapies: In addition to its role in vaccination, the Influenza B Virus Nucleoprotein Recombinant holds potential in antiviral therapies. The recombinant protein's ability to provoke immune responses can be harnessed for the development of immunotherapies. Monoclonal antibodies derived from the Nucleoprotein Recombinant may offer targeted treatments, providing a dynamic approach to mitigating the impact of Influenza B infections. Challenges and Future Directions: Despite the promises held by the Nucleoprotein Recombinant, challenges persist. The virus's ability to undergo genetic reassortment and antigenic drift requires ongoing vigilance and adaptability in recombinant strategies. Considerations of vaccine safety, efficacy, and public acceptance demand continual exploration to optimize the translational success of Nucleoprotein Recombinant-based interventions. Influenza B Virus Nucleoprotein Recombinant stands as a beacon in the scientific quest against influenza, offering a pathway to a more comprehensive and resilient immunity. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies position it as a central player. As researchers delve deeper into the molecular intricacies of Nucleoprotein Recombinant, they not only fortify our defenses against Influenza B but potentially pave the way for a paradigm shift in our approach to influenza prevention and control, influencing the landscape of global health preparedness. | |
| Precautions | |
| IBSP Human, HEK is for research use only and not for use in diagnostic or therapeutic procedures. | |
Background |
1. Structural Diversity: Research on IBSP often delves into its structural characteristics. IBSP is known for its rich sialic acid content and multiple functional domains, including an RGD cell-binding domain and polyglutamic acid stretches. These structural features enable IBSP to interact with various cells, affecting adhesion and migration. 2. Mineralization Regulator: A significant focus of research is IBSP's role in mineralization. It acts as a nucleator for calcium phosphate crystals, providing a scaffold for bone formation. Understanding how IBSP influences mineralization is crucial for insights into bone health and diseases like osteoporosis. 3. Cell Signaling: Research papers explore IBSP's involvement in cell signaling pathways. IBSP has been linked to angiogenesis, inflammation, and cellular differentiation. Investigating these signaling pathways sheds light on its broader physiological roles. 4. Biomedical Implications: Studies often discuss the biomedical implications of IBSP. Researchers investigate its potential roles in bone disorders such as osteoporosis and periodontal disease. Additionally, IBSP's involvement in tumor metastasis and dental tissue regeneration is a subject of interest. 5. Recombinant IBSP: The use of recombinant IBSP in research is a significant topic. Researchers utilize recombinant IBSP to explore its functions, interactions, and potential therapeutic applications. This allows for controlled experiments and insights into IBSP's behavior. 6. Diagnostics and Therapeutics: Research papers may discuss the diagnostic and therapeutic potential of IBSP. Understanding its roles in health and disease can lead to the development of diagnostic markers and therapeutic interventions, particularly in the context of bone and dental health. 7. Clinical Relevance: Some research may focus on the clinical relevance of IBSP. This could include studies on patient populations with IBSP mutations or alterations, aiming to understand how variations in IBSP may contribute to specific medical conditions. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from ADMEbio to advance their research.
Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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ADMEbio Team
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ADMEbio Team
