Recombinant Chikungunya Virus Non-Structural Polyprotein，Partial (P1234) Protein (His)

Name: Recombinant Chikungunya Virus Non-Structural Polyproteinï¼ŒPartial (P1234) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03747P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Chikungunya Virus Non-Structural Polyprotein，Partial (P1234) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8JUX6
Target Symbol	Q8JUX6
Synonyms	Polyprotein P1234; P1234; Non-structural polyprotein) [Cleaved into: Polyprotein P123; P123); mRNA-capping enzyme nsP1; EC 2.1.1.-; EC 2.7.7.-; Non-structural protein 1); Protease nsP2; EC 3.1.3.33; EC 3.4.22.-; EC 3.6.1.15; EC 3.6.4.13; Non-structural protein 2; nsP2); Non-structural protein 3; nsP3; EC 3.1.3.84); RNA-directed RNA polymerase nsP4; EC 2.7.7.19; EC 2.7.7.48; Non-structural protein 4; nsP4)]
Species	Chikungunya virus (strain S27-African prototype) (CHIKV)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DTVLETDIASFDKSQDDSLALTALMLLEDLGVDHSLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFVNTLLNITIASRVLEDRLTKSACAAFIGDDNIIHGVVSDELMAARCATWMNMEVKIIDAVVSQKAPYFCGGFILHDIVTGTACRVADPLKRLFKLGKPLAAGDEQDEDRRRALADEVVRWQRTGLIDELEKAVYSRYEVQGISVVVMSMATFASSRSNFEKLRGPVVTLYGGPK
Expression Range	2228-2474aa
Protein Length	Partial
Mol. Weight	31.1kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.; The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs. As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins.; Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and guanylyltransferase. mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. NsP1 is also needed for the initiation of the minus-strand RNAs synthesis. At the initiation of virus replication, mediates the assembly of the viral replication complex made of the non-structural proteins, the association of this complex with the inner face of the plasma membrane and the formation of membranous spherules that serve as replication complex factories. Forms the neck of these spherules with a central channel for mediating communication and the passage of RNA, nucleotides, and small proteins between the viral replication complex and the host cytoplasm. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell.; Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities. NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates. The C-terminus harbors a protease that specifically cleaves the polyproteins and releases the mature proteins. Required for the shutoff of minus-strand RNAs synthesis. Specifically inhibits the host IFN response by promoting the nuclear export of host STAT1. Also inhibits host transcription by inducing the rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable).; Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis. Displays mono-ADP-ribosylhydrolase activity. ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication. Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs. The nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA (Probable).; RNA dependent RNA polymerase. Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs. The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs.
Subcellular Location	[Polyprotein P1234]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [Polyprotein P123]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [mRNA-capping enzyme nsP1]: Host cytoplasmic vesicle membrane; Lipid-anchor. Host cell membrane; Lipid-anchor; Cytoplasmic side. Host cell projection, host filopodium.; [Protease nsP2]: Host cytoplasmic vesicle membrane; Peripheral membrane protein. Host nucleus. Host cytoplasm.; [Non-structural protein 3]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [RNA-directed RNA polymerase nsP4]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.
Database References	KEGG: vg:956309

Gene Functions References

Chikungunya virus (CHIKV) nonstructural protein nsP3 (Nsp3)C-terminal hypervariable domain (HVD) can bind cytoskeletal proteins, including CD2AP, SH3KBP1, CAPZA1, CAPZA2 and CAPZB. Binding site is mapped to the second SH3 ligand-like element in Nsp3 HVD. Mutation of the short binding element hampered the ability of the virus to establish infection. PMID: 29702546
In summary, nsP3 can form uniquely stable granular structures that persist long-term within the host cell. PMID: 29875241
Therefore, the opal termination codon at the end of the nsp3 gene plays an important role in Chikungunya virus pathogenesis, independently of effects on viral replication. PMID: 29138302
Two non-structural proteins, namely, nsP2 and nsP3 were found to exhibit RNAi suppressor activity. PMID: 27901124
Cys478 residue in the active site of CHIKV nsP2 is indispensable for P1234 processing. PMID: 27845418
Date show that viral nonstructural protein nsP3 (nsP3) mono(ADP-ribosyl)hydrolase activity is critical for Chikungunya virus (CHIKV) replication in both vertebrate hosts and insect vectors, and for virulence in mice. PMID: 28143925
data show that the previously described consensus sequence PXRPXR for amphiphysin SH3 ligands is inaccurate and instead define it as an extended Class II binding motif PXXPXRpXR, where additional positive charges between the two constant arginine residues can give rise to extraordinary high SH3 binding affinity. PMID: 27268056
Site-directed mutagenesis showed that the mosquito Rin-Chikungunya virus nsP3 interaction involved the NTF2-like domain of Rin and two conserved TFGD repeats in the C-terminal variable domain of nsP3. PMID: 26384002
This study shows the essential role and novel function of nsP2 in maintaining alphavirus replication complex fidelity. PMID: 26311883
Molecular docking analysis/molecular dynamics simulations leading to enzyme inhibitors targeting nsP3 macro domain of chikungunya virus. PMID: 24756552
P718G or E116K mustation of nsp2 markedly reduced RNA synthesis. PMID: 25552719
Authors have identified novel interactions between Chikungunya virus nsP3 or nsP4 proteins with the host stress-pathway chaperone HSP-90 protein. PMID: 24388965
Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity. PMID: 24407286
Results show that nsP2 mutation P718S only in combination with KR649AA or adaptive mutation D711G allowed noncytopathic replicon RNA replication. PMID: 23864632
Authors conclude that BST-2 tethers chikungunya virus like particles on the host cell plasma membrane and identify viral nsP1 protein as a novel BST-2 antagonist. PMID: 23411007
Chikungunya virus nsP3 blocks stress granule assembly by recruitment of G3BP into cytoplasmic foci PMID: 22837213
Viral nsP2 interacts with hostibonucleoprotein K and ubiquilin 4 protein. PMID: 22258240
Expression of individual CHIKV nonstructural proteins (nsPs) showed that nsP2 was a potent inhibitor of IFN-induced JAK-STAT signaling. PMID: 20686047

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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