Recombinant Sars-Cov-2 Replicase Polyprotein 1Ab (REP) Protein (His)

Name: Recombinant Sars-Cov-2 Replicase Polyprotein 1Ab (REP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06604P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Sars-Cov-2 Replicase Polyprotein 1Ab (REP) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P0DTD1
Target Symbol	REP
Synonyms	(pp1ab)(ORF1ab polyprotein)(Leader protein)(Non-structural protein 1)(nsp1)(nsp2)(p65 homolog)(Non-structural protein 3)(nsp3)(PL2-PRO)(Papain-like proteinase)(PL-PRO)(nsp4)(3CL-PRO)(3CLp)(Main protease)(Mpro)(Non-structural protein 5)(nsp5)(SARS coronavirus main proteinase)(nsp6)(nsp7)(nsp8)(nsp9)(nsp10)(Growth factor-like peptide)(GFL)(Pol)(RdRp)(Non-structural protein 12)(nsp12)(Hel)(Non-structural protein 13)(nsp13)(ExoN)(Guanine-N7 methyltransferase)(Non-structural protein 14)(nsp14)(NendoU)(Non-structural protein 15)(nsp15)(Non-structural protein 16)(nsp16)
Species	Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Expression System	Baculovirus
Tag	C-6His
Target Protein Sequence	AVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQ
Expression Range	1-601aa
Protein Length	Full Length
Mol. Weight	70.0 kDa
Research Area	Microbiology
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

Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.; Inhibits host translation by associating with the open head conformation of the 40S subunit. The C-terminus binds to and obstructs ribosomal mRNA entry tunnel. Thereby inhibits antiviral response triggered by innate immunity or interferons. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence.; May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.; Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Cleaves preferentially ISG15 from antiviral protein IFIH1 (MDA5), but not DDX58 (RIG-I). Can play a role in host ADP-ribosylation by binding ADP-ribose.; Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.; Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production.; Plays a role in viral RNA synthesis. Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.; Plays a role in viral RNA synthesis. Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. Interacts with ribosome signal recognition particle RNA (SRP). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses.; May participate in viral replication by acting as a ssRNA-binding protein. Interacts with ribosome signal recognition particle RNA (SRP). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses.; Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.; Responsible for replication and transcription of the viral RNA genome.; Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. Binds to host TBK1 and inhibits TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production.; Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.; Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR. Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors.; Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. May disrupt host mRNA splicing in nucleus by interacting with pre-mRNA Recognition Domains ofthe U1 and U2 snRNAs.

Subcellular Location

[Host translation inhibitor nsp1]: Host cytoplasm.; [Non-structural protein 2]: Host cytoplasm. Host endosome.; [Papain-like protease nsp3]: Host membrane; Multi-pass membrane protein. Host cytoplasm.; [Non-structural protein 4]: Host membrane; Multi-pass membrane protein. Host cytoplasm.; [3C-like proteinase nsp5]: Host cytoplasm. Host Golgi apparatus.; [Non-structural protein 6]: Host membrane; Multi-pass membrane protein.; [Non-structural protein 7]: Host cytoplasm, host perinuclear region. Host cytoplasm. Host endoplasmic reticulum.; [Non-structural protein 8]: Host cytoplasm, host perinuclear region. Host cytoplasm. Host endoplasmic reticulum.; [Non-structural protein 9]: Host cytoplasm, host perinuclear region. Host cytoplasm. Host endoplasmic reticulum.; [Non-structural protein 10]: Host cytoplasm, host perinuclear region. Host cytoplasm. Host endoplasmic reticulum.; [Proofreading exoribonuclease nsp14]: Host cytoplasm. Host endoplasmic reticulum. Host endoplasmic reticulum.; [Helicase nsp13]: Host endoplasmic reticulum-Golgi intermediate compartment.; [Uridylate-specific endoribonuclease nsp15]: Host cytoplasm, host perinuclear region.; [2'-O-methyltransferase nsp16]: Host nucleus. Host cytoplasm.

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.