Analytical Data
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Gene name
Bm1_01445
- Application
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Alternative Names
tRNA (guanine(46)-N(7))-methyltransferase tRNA(m7G46)-methyltransferase
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Species
Brugia malayi
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A8NFF0
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Expression Region
1-258aa
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Molecular Weight
36.3 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
Bm1_01445 is a putative recombinant protein derived from Bombyx mori, commonly known as the silkworm, which has garnered significant interest in the field of molecular biology and biotechnology. This protein’s study is driven by the need to understand its biological functions and potential applications, particularly in the areas of silk production, pest resistance, and biopharmaceutical development. The silkworm has a well-established role in the textile industry, but its genetic and protein characteristics are also being explored for innovative approaches to enhance silk quality and yield. Additionally, Bm1_01445 may exhibit unique enzymatic activities or cellular interactions that could be leveraged in genetic engineering or synthetic biology. Current research involves gene cloning, protein expression, and functional analysis, aiming to elucidate its structure-function relationship and possible utility in creating transgenic organisms with desirable traits. Understanding the role of Bm1_01445 in silkworm physiology could lead to advancements in sustainable agriculture and innovative biomaterials, as well as provide insights into the conservation of beneficial insect species. Thus, the study of this recombinant protein is not only important from a scientific perspective but also holds promise for practical applications in various biotechnological fields.
