Recombinant Bovine Viral Diarrhea Virus Genome Polyprotein Protein (His)

Name: Recombinant Bovine Viral Diarrhea Virus Genome Polyprotein Protein (His)
Brand: Beta LifeScience
SKU: BLC-05118P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Bovine Viral Diarrhea Virus Genome Polyprotein Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q01499
Target Symbol	Q01499
Synonyms	Genome polyprotein
Species	Bovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease virus)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	MELITNELLYKTYKQKPVGVEEPVYDQAGNPLFGERGAIHPQSTLKLPHKRGERNVPTSLASLPKRGDCRSGNSKGPVSGIYLKPGPLFYQDYKGPVYHRAPLELFEEGSMCETTKRIGRVTGSDGKLYHIYICIDGCITVKSATRSHQRVLRWVHNRLDCPLWVTSC
Expression Range	1-168aa
Protein Length	Partial
Mol. Weight	25.0 kDa
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.
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	Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation.; Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Plays also a role in transcription regulation. Protects the incoming virus against IFN-induced effectors.; Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis.; Plays an essential role in the virus replication cycle by acting as a viroporin. Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules. Forms a leader sequence to properly orient NS2 in the membrane.; Uncleaved NS2-3 is required for production of infectious virus.; Plays a role in the regulation of viral RNA replication.; Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity.; Acts as a cofactor for the NS3 protease activity.; Induces a specific membrane alteration that serves as a scaffold for the virus replication complex.; Replicates the viral (+) and (-) genome.
Subcellular Location	[Capsid protein C]: Virion.; [E(rns) glycoprotein]: Host membrane; Peripheral membrane protein. Virion membrane; Peripheral membrane protein.; [Envelope glycoprotein E2]: Host cell surface. Virion membrane.; [Cysteine protease NS2]: Host membrane; Multi-pass membrane protein.; [Serine protease NS3]: Host cytoplasm.; [Non-structural protein 4B]: Host cytoplasm.; [Non-structural protein 5A]: Host cytoplasm.
Protein Families	Pestivirus polyprotein family

FAQs

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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.

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