Recombinant Escherichia Phage T7 Dna Primase/Helicase (4) Protein (His&Myc)

Name: Recombinant Escherichia Phage T7 Dna Primase/Helicase (4) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-11278P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Enterobacteria phage T7 (Bacteriophage T7) 4.

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 Escherichia Phage T7 Dna Primase/Helicase (4) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P03692
Target Symbol	4
Synonyms	4; DNA primase/helicase; EC 2.7.7.-; EC 3.6.4.12; Gene product 4; Gp4
Species	Escherichia phage T7 (Bacteriophage T7)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	KKIVVTEGEIDMLTVMELQDCKYPVVSLGHGASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANECHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCTGINDKTLGARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRVRLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDVIILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRPVSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETGWLEPSSYS
Expression Range	151-548aa
Protein Length	Partial
Mol. Weight	51.3 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.
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

ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination. The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis. ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA. Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange. Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present.

Database References

KEGG: vg:1261046

Gene Functions References

structural model of a bacteriophage T7 DNA helicase-DNA polymerase complex PMID: 22977246
Zinc-binding domain of the bacteriophage T7 DNA primase modulates binding to the DNA template PMID: 23024359
Data show that tryptophans Trp-42, -97, and -147 play different but essential roles in T7 DNA primase. PMID: 22605336
The ligation state of the zinc ion was examined by X-ray absorption spectroscopy and biochemical analysis of genetically altered primases, was analysed. PMID: 19206208
thioredoxin-binding domain of T7 DNA polymerase is the site of interaction of the phage-encoded helicase/primase (gp4) and ssDNA binding protein (gp2.5) PMID: 15795374
residues Glu-157, Glu-159, Asp-161, Asp-207, Asp-209, and Asp-237 are essential for binding affinity for ATP PMID: 15917241
The switch in contacts between Asp(263) and Tyr(411), Lys(408), or Arg(404) in helix E of the adjacent subunit results in conformational changes that modulate helicase and primase activity. PMID: 19574219

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.