Analytical Data
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Gene name
virE2
- Application
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Alternative Names
virE2;Single-strand DNA-binding Protein
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A3W9
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Expression Region
316-533aa
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AA Sequence
NRAHNRQFPTATVNMGQQPDGQGGLTRDRHVSVEFLMQSAPNSPWAQALKKGELWDRVQLLARDGNRYLSPHRLEYSDPEHFTELMNRVGLPASMGRQSHAASIKFEKFDAQAAVIVINGPELRDIHDLSPENLQNVSTKDVIVADRNENGQRTGTYTSVAEYERLQLRLPADAAGVLGEAADKYSRDFVRPEPASRPISDSRRIYESRPRSQSVNSF
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Molecular Weight
31.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
VirE2 protein, encoded by the Agrobacterium tumefaciens pTi virulence plasmid, plays a crucial role in the transformation of plant cells by acting as a key component in the delivery of T-DNA into the host genome. Understanding the structure and function of VirE2 is essential for exploiting its properties in biotechnology and genetic engineering. Research has shown that VirE2 forms a complex with T-DNA during its transport, facilitating nuclear import and integration into the plant's DNA. This interaction is vital for the Agrobacterium-mediated genetic transformation process, which has significant applications in generating transgenic plants and improving agricultural traits. Investigating the biochemical properties and interactions of VirE2 can enhance our understanding of its mechanism of action and enable the development of novel tools for plant transformation. Furthermore, the potential use of VirE2 as a vector for delivering genetic material into eukaryotic cells expands its significance beyond plant biology into broader fields such as medicine and biotechnology. Recent studies focus on the optimization of VirE2 for increased efficiency and specificity in delivering therapeutic genes, highlighting its importance in the advancement of gene therapy methods. Overall, the exploration of VirE2 as a recombinant protein not only sheds light on fundamental plant-pathogen interactions but also opens avenues for innovative biotechnological applications.











