Recombinant Hepatitis E Virus Genotype 1 Non-Structural Polyprotein Porf1 (ORF1) Protein (His)

Name: Recombinant Hepatitis E Virus Genotype 1 Non-Structural Polyprotein Porf1 (ORF1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09821P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Hepatitis E Virus Genotype 1 Non-Structural Polyprotein Porf1 (ORF1) 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	P33424
Target Symbol	ORF1
Synonyms	ORF1; Non-structural polyprotein pORF1 [Includes: Methyltransferase; EC 2.1.1.-; EC 2.7.7.-); Putative papain-like cysteine protease; PLP; EC 3.4.22.-); NTPase/helicase; EC 3.6.4.-); RNA-directed RNA polymerase; RdRp; EC 2.7.7.48)]
Species	Hepatitis E virus genotype 1 (isolate Human/Pakistan/Sar-55) (HEV-1)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	EVFWNHPIQRVIHNELELYCRARSGRCLEIGAHPRSINDNPNVVHRCFLRPAGRDVQRWYTAPTRGPAANCRRSALRGLPAADRTYCFDGFSGCNFPAETGIALYSLHDMSPSDVAEAMFRHGMTRLYAALHLPPEVLLPPGTYRTASYLLIHDGRRVVVTYEGDTSAGYNHDVSNLRSWI
Expression Range	60-240aa
Protein Length	Partial
Mol. Weight	24.4kDa
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	Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure.; Papain-like cysteine protease: May participate in the processing of polyprotein pORF1 together with cellular proteases and the cleavage of capsid protein ORF2.; NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities. Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs. Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure. Participates also in viral genome replication, RNA translocation and genome packaging/unpackaging.; RNA-directed RNA polymerase: Plays an essential role in the virus replication. Binds to the 3'-end of the genomic RNA to initiate viral replication.
Subcellular Location	Host cytoplasm.
Protein Families	Hepevirus non-structural 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.