Product Details

Purity

>85% (SDS-PAGE)

Target Names

PB2

Uniprot No.

P03428

Alternative Names

PB2Polymerase basic protein 2; RNA-directed RNA polymerase subunit P3

Species

Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS.

Gene References into Functions

Viral polymerase activity, viral replication, and pathogenicity in mice were enhanced due to the substitution of D701N in the PB2 protein. PMID: 29717109
Activated PKCdelta interacts with the polymerase subunit PB2 and phospho-regulates NP oligomerization and RNP assembly during influenza A virus infection. PMID: 28758638
The role of the 627 domain in H1N1 PB2 polymerase function. PMID: 28122973
PB2 V661A and V683T/A684S are involved in enhanced polymerase activity at low temperature. PMID: 26018156
By recruiting importin alpha3 or alpha7 in the absence of importin beta, PB2 reduces the complexity of adaptor-mediated import to a pseudo-bimolecular reaction, thereby acquiring a kinetic advantage over classical nuclear localization signal cargos. PMID: 25599645
From these results, we suggest that influenza virus polymerase activity may be regulated through the interaction between PB2 627-domain and RNA and that consequently host adaptation of the virus may be influenced. PMID: 24875650
Mutations in PB2 gene is associated with virulence. PMID: 24699508
PB2-588I enhances 2009 H1N1 pandemic influenza virus virulence by increasing viral replication and exacerbating PB2 inhibition of beta interferon expression. PMID: 24335306
The substitution of glutamic acid (E) for lysine (K) at position 627 of the PB2 protein of avian H5N1 viruses has been identified as a virulence and host range determinant for infection of mammals. PMID: 23864613
Computational studies on the substrate interactions of influenza A virus PB2 subunit PMID: 22957044
our findings indicate that the PB2 C-terminal domain has multiple effects on RdRp activities besides importin binding. PMID: 22146492
271A, 590S, and 591R of PB2 is critical for viral replication and virulence. PMID: 22072752
Amino acid residue 271, 588, 701 and 636 of PB2 contributors to host-specific activity. PMID: 21471313
These findings demonstrate that the viral polymerase plays an important role for regulating host anti-viral response through the binding to IPS-1 and inhibition of IFNbeta production PMID: 20699220
a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals PMID: 20700447
Influenza virus A PB2 protein interacts with MAVS and inhibits MAVS-mediated beta interferon expression. PMID: 20538852
2009 H1N1 virus has acquired second-site suppressor mutations in its PB2 polymerase subunit that convey enhanced polymerase activity in human cells PMID: 19995968
The C-terminal domain protein (amino-acid residues 535-759) of the PB2 subunit of the RNA-dependent RNA polymerase from the influenza A virus has been expressed as a soluble protein and crystallized. PMID: 19194006
Adaptive mutations in PB2 cause enhanced polymerase activity and promote high virulence. PMID: 19403683

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Subcellular Location

Virion. Host nucleus. Host mitochondrion.

Protein Families

Influenza viruses PB2 family

Database Links

KEGG: vg:956536

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Recombinant Influenza A virus Polymerase basic protein 2 (PB2), partial

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