Analytical Data
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Gene name
ynaB
- Application
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Alternative Names
ynaB; BSU17500; Uncharacterized protein YnaB
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Species
Bacillus subtilis
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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
P94480
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Expression Region
1-144aa
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Molecular Weight
32.8 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
YnaB is a protein of significant interest in bacterial physiology and biochemistry, primarily due to its potential role in stress responses and cellular signaling. Discovered in *Escherichia coli*, YnaB has been implicated in the regulation of biofilm formation and adaptation to changing environmental conditions, such as nutrient availability and temperature fluctuations. The study of YnaB offers insights into the mechanisms through which bacteria respond to external stimuli, which is crucial for understanding pathogenicity and the development of antibiotic resistance. The recombinant expression of YnaB enables researchers to investigate its structural and functional properties in detail, facilitating the exploration of its interactions with other biomolecules. Through techniques such as X-ray crystallography and NMR spectroscopy, scientists aim to elucidate the protein's three-dimensional structure, which can reveal its biochemical pathways and potential as a target for novel therapeutic strategies. Furthermore, understanding YnaB's role could shed light on broader bacterial survival mechanisms, ultimately contributing to advancements in microbial biotechnology and medical research.
