IBV-NP

Influenza B Virus Nucleoprotein Recombinant
Cat. No.
BT27165
Source

E. coli.

Synonyms
Appearance

Sterile Filtered clear solution.

Purity
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Influenza B Virus Nucleoprotein produced in E. coli having a Mw of 76.8kDa. IBV-NP is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.

Product Specs

Description
Recombinant Influenza B Virus Nucleoprotein, with a molecular weight of 76.8kDa, is produced in E. coli. This protein is fused with a 6xHis tag at its C-terminal and undergoes purification using a proprietary chromatographic technique.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The IBV-NP protein solution is formulated in 25mM K2CO3 and PBS.
Stability
For short-term storage (2-4 weeks), the protein should be stored at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Source

E. coli.

Amino Acid Sequence

HMSNMDIDGMNTGTIDKTPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPDRTTTSSE

DDVGRKAQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILL

AATDDKKTEFQKKKNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIRITFLKEEVKT

MYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTVPRRSGATGV

AIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRN

PGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATP

VSILRMGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGA

ALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADV

KGNLLKMMNDSMAKKTSGNAFIGKKMFQISDKNKTNPIEIPIKQTIPNFFFGRDTAEDYDDLDYLE.

Product Science Overview

Introduction

Influenza B virus (IBV) is a significant cause of seasonal flu epidemics, affecting millions of people worldwide each year. Unlike Influenza A, which can infect multiple species, Influenza B primarily infects humans, making it a critical target for vaccine development and antiviral research. One of the key components in the study of IBV is the nucleoprotein (NP), which plays a crucial role in the virus’s replication and host adaptation.

Structure and Function of Influenza B Nucleoprotein

The nucleoprotein (NP) of Influenza B virus is a multifunctional protein that encapsidates the viral RNA genome, protecting it from nucleases and forming the ribonucleoprotein (RNP) complex . This complex is essential for the transcription and replication of the viral genome. The NP contains two nuclear localization signals (NLSs), which facilitate the transport of the RNP complex into the nucleus of the host cell .

Recombinant Nucleoprotein

Recombinant nucleoproteins are artificially produced proteins that mimic the natural nucleoproteins of the virus. These recombinant proteins are typically expressed in host cells, such as baculovirus-insect cells, to ensure high yield and purity . The recombinant Influenza B nucleoprotein is often tagged with a polyhistidine tag to facilitate purification and detection .

Applications in Research and Vaccine Development

Recombinant Influenza B nucleoprotein is a valuable tool in virology research. It allows scientists to study the structure and function of the NP in detail, providing insights into the mechanisms of viral replication and host adaptation. Additionally, recombinant NPs are used in the development of diagnostic assays and vaccines. By understanding how the NP interacts with the host cell machinery, researchers can design more effective antiviral drugs and vaccines .

Stability and Storage

Recombinant proteins, including Influenza B nucleoprotein, are typically lyophilized (freeze-dried) to ensure stability during storage and transport . These proteins are stable for up to twelve months when stored at -20°C to -80°C under sterile conditions. It is important to avoid repeated freeze-thaw cycles to maintain the protein’s integrity .

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