Recombinant Escherichia Phage T7 T7 Rna Polymerase (1) Protein (His&Myc)

Name: Recombinant Escherichia Phage T7 T7 Rna Polymerase (1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00620P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Escherichia Phage T7 T7 Rna Polymerase (1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00573
Target Symbol	1
Synonyms	(DNA-directed RNA polymerase)
Species	Escherichia phage T7 (Bacteriophage T7)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	PPKPWTGITGGGYWANGRRPLALVRTHSKKALMRYEDVYMPEVYKAINIAQNTAWKINKKVLAVANVITKWKHCPVEDIPAIEREELPMKPEDIDMNPEALTAWKRAAAAVYRKDKARKSRRISLEFMLEQANKFANHKAIWFPYNMDWRGRVYAVSMFNPQGNDMTKGLLTLAKGKPIGKEGYYWLKIHGANCAGVDKVPFPERIKFIEENHENIMACAKSPLENTWWAEQDSPF
Expression Range	274-509aa
Protein Length	Partial
Mol. Weight	34.6 kDa
Research Area	Signal Transduction
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	Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.
Protein Families	Phage and mitochondrial RNA polymerase family
Database References	KEGG: vg:1261050

Gene Functions References

Using correlation analysis, it was found that the promoter strength characterized by reporter gene expression was closely correlated with rupture force and the binding percentage of T7 RNA polymerase by force spectroscopy. PMID: 29187520
From the docking of the minimum energy representative structures of T7 lysozyme at different pH strengths (obtained from the free energy landscape analysis) with T7RNAP structures at same pH strengths, we saw strong interaction patterns at pH 7.9 and pH 5. PMID: 28545576
Data suggest that comparative transcriptional fidelities/mutation rates for DNA-directed RNA polymerases are as follows: human mitochondrial POLRMT [2x10(-5)]; Saccharomyces cerevisiae mitochondrial Rpo41 [6x10(-6)]; phage T7 single-subunit RNA polymerase [2x10(-6)]. PMID: 28882896
Molecular dynamics simulation study described the behavior of the two magnesium ions in RNAP activity during genetic transcription. PMID: 28205291
The control of the discrimination between dNTP and rNTP in DNA and RNA polymerases has been described. PMID: 27480935
The study provides evidence that the intrinsic infidelity of T7 RNAP in transcription brings significant phenotypic consequences, observed as frameshift mutation restoration and the production of a heterogenous population of the full-length protein. PMID: 25824942
We show here that DNA-protein cross-links constitute strong but not absolute blocks to in vitro transcription catalyzed by T7 RNAP. PMID: 22235136
Hydrogen bonds of RNA polymerase play an important role in the efficiency of transcription. PMID: 22044042
introducing a nuclear transgene, ST7, encoding a light-regulated plastid-targeted T7RNAP by cross-pollination. PMID: 15517992
T7 promoter-polymerase interaction weakening facilitates promoter release PMID: 15711016
An amino acid substitution weakens promoter binding but markedly reduces abortive cycling over a variety of initial sequences. PMID: 15831591
structure activity relationship PMID: 16301518
Active T7RNAP elongation by showing that both rapidly elongating and halted complexes are equally sensitive to pyrophosphate. PMID: 16516229
Collapse of the DNA from the downstream end of the bubble is a major contributor to the characteristic instability of the abortive T7 RNA polymerase transcription complex. PMID: 16790422
Poto-regulation of transcription reaction by azobenzene-tethered promoter was attributed to the change of binding property of RNAP to the promoter by trans-cis isomerization of azobenzene. PMID: 17150558
transition to an elongation complex by T7 RNA polymerase is a multistep process PMID: 17548349
site-specifically tethered chemical nucleases and functional characterization of directed T7 RNAP mutants to both reveal the architecture of the duplex DNA PMID: 17580086
G-rich sequences located in the transcribed strand do not affect transcription by either polymerase, but when the sequences are located in the non-transcribed strand, they partially arrest both polymerases PMID: 18292094
study reports crystal structures of T7 RNAP bound to promoter DNA containing either a 7- or an 8-nucleotide (nt) RNA transcript that illuminate intermediate states along the transition pathway PMID: 18948533

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.