Analytical Data
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Gene name
ecoRVM
- Application
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Alternative Names
ecoRVM；Type II methyltransferase M.EcoRV
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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
P04393
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Expression Region
1-298aa
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AA Sequence
MKDKVFVPPIKSQGIKTKLVPCIKRIVPKNFNGVWVEPFMGTGVVAFNVAPKDALLCDTNPHLISFYNALKNKDITGDLVKDFLYREGEKLLLSNGEYYYEVRERFNNYKEPLDFLFLNRSCFNGMIRFNSKGGFNVPFCKKPNRFAQAYITKISNQVDRISEIISKGNYTFLCQSFEKTIGMVNRDDVVYCDPPYIGRHVDYFNSWGERDERLLFETLSSLNATFITSTWHHNDYRENKYVRDLWSSFRILTKEHFYHVGASEKNRSPMVEALITNIAKDIIDHIEKSSGDILVIEE
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Molecular Weight
50.6 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
Related Products
Protein Description
The study of ecoRVM, a recombinant protein derived from the EcoRVM restriction enzyme, has garnered significant attention due to its potential applications in molecular biology and biotechnology. As a member of the Type II restriction endonucleases, ecoRVM plays a critical role in gene editing, cloning, and the development of novel biotechnological tools. Its specificity for particular DNA sequences makes it invaluable for precise genetic manipulation. Additionally, the ability to produce ecoRVM in recombinant form allows researchers to obtain large quantities of the enzyme, facilitating extensive studies on its structure-function relationship and mechanisms of action. Understanding ecoRVM's properties can lead to advances in areas such as synthetic biology, therapeutic development, and genetic engineering, enabling more efficient and accurate modifications of genetic material. Furthermore, the exploration of ecoRVM's potential limitations and advantages compared to other restriction enzymes will enhance its usability in various applications, contributing to advancements in genetic research and biotechnological innovation. As the field of genome editing continues to evolve, the relevance of ecoRVM and similar recombinant proteins will likely increase, propelling further research and development to exploit their full potential in scientific and medical applications.
