Analytical Data
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Gene name
ecoRVM
- Application
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Alternative Names
Adenine-specific methyltransferase EcoRV
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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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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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 recombinant proteins has gained significant attention in the field of biotechnology and molecular biology due to their potential applications in various industries, including pharmaceuticals, environmental science, and synthetic biology. EcoRVM is a type of restriction enzyme derived from the bacterium Escherichia coli, specifically known for its ability to recognize and cleave specific DNA sequences. Researchers are particularly interested in ecoRVM because of its unique properties, such as its high specificity and efficiency in DNA manipulation, which makes it a valuable tool for genetic engineering and molecular cloning. Furthermore, understanding the mechanisms behind ecoRVM’s function can lead to advancements in genome editing techniques, such as CRISPR-Cas systems. The exploration of recombinant forms of ecoRVM also paves the way for enhancing its functionality and stability, potentially leading to more robust applications in genetic research and biotechnology. As the demand for efficient DNA modification tools continues to grow, the investigation into ecoRVM recombinant proteins promises to contribute significantly to genetic innovation and molecular therapeutics, facilitating breakthroughs in gene therapy, personalized medicine, and bioproduction systems.
