Analytical Data
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Gene name
virD2
- Application
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Alternative Names
virD2；T-DNA border endonuclease VirD2
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Species
Human
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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
P18592
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Expression Region
1-447aa
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AA Sequence
MPDRAQVIIRIVPGGGTKTLQQIINQLEYLSRKGRLELQRSARHLDIPLPPDQIHELARSWVQETGTYDESQPDEERQQELTTHIIVSFPAGTSQVAAYAASREWAAEMFGSGAGGGRYNYLTAFHIDRDHPHLHVVVNRRELLGHGWLKISRRHPQLNYDALRIKMAEISLRHGIALDASRRAERGITERPITYAQYRRLEREQARQIRFEDADLEQSSPQGDHPEFSQPFDTSPFEASAGGPEDMPRPNNRQNESQVHLQEPAGVSNEAGVLVRVALETERLAQPFVSETILADDIGSGSSRVAEGRVESANRTPDIPRAATEAATHTTHDRQRRAKRPHDDDGGPSGAKRVTLEGIAVGPQANAGEQDGSSGPLVRQAGTSRPSPPTATTRASTATDSLSATAHLQQRRGVLSKRPREDDDGEPSERKRERDERSKDGRGGNRR
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Molecular Weight
57.0 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
VirD2 is a key protein involved in the process of T-DNA transfer during Agrobacterium tumefaciens-mediated plant transformation, playing a crucial role in plant biotechnology. As a component of the Virulence (Vir) proteins, VirD2 is responsible for the recognition and processing of DNA to form the T-complex, which is essential for the successful insertion of foreign DNA into the plant genome. The protein possesses nuclease activity, facilitating the cleavage of the T-DNA from the plasmid, and is also involved in the formation of a covalent bond with the 5' end of the T-DNA, which is vital for its translocation to plant cells. Furthermore, VirD2 interacts with other Vir proteins to form a transport channel through the bacterial and plant cell membranes. The study of VirD2 has significant implications not only for understanding the mechanistic aspects of Agrobacterium infection but also for enhancing the efficiency of genetic engineering techniques in plants. Research has focused on characterizing its functional domains, exploring its interactions with other proteins, and optimizing its role in T-DNA transfer to improve crop traits and develop genetically modified organisms (GMOs) for agriculture. Additionally, due to its ability to facilitate DNA transfer, VirD2 has been examined for potential applications in gene therapy and synthetic biology, highlighting its versatility and importance in both fundamental research and applied sciences. Understanding the nuances of VirD2's activity can lead to advancements in biotechnological applications, making it a pivotal area of study in the quest for improved agricultural practices and sustainable crop production.
