Analytical Data
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Gene name
BAR1
- Application
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Alternative Names
BAR1；BRCA1-associated RING domain Protein 1
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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
P12630
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Expression Region
43-395aa
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AA Sequence
MYYATTLDIGTPSQSLTVLFDTGSADFWVMDSSNPFCLPNSNTSSYSNATYNGEEVKPSIDCRSMSTYNEHRSSTYQYLENGRFYITYADGTFADGSWGTETVSINGIDIPNIQFGVAKYATTPVSGVLGIGFPRRESVKGYEGAPNEYYPNFPQILKSEKIIDVVAYSLFLNSPDSGTGSIVFGAIDESKFSGDLFTFPMVNEYPTIVDAPATLAMTIQGLGAQNKSSCEHETFTTTKYPVLLDSGTSLLNAPKVIADKMASFVNASYSEEEGIYILDCPVSVGDVEYNFDFGDLQISVPLSSLILSPETEGSYCGFAVQPTNDSMVLGDVFLSSAYVVFDLDNYKISLAQA
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Molecular Weight
44.4 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
BAR1 (Bacteria Artificially Recombinant Protein 1) has emerged as a significant focus in molecular biology and biotechnology due to its potential applications in various fields, including medicine, agriculture, and industrial biotechnology. Researchers have been exploring BAR1 for its role in protein engineering, aiming to develop novel therapeutic proteins with desirable properties such as enhanced stability, efficacy, and specificity. The ability to manipulate BAR1 allows scientists to understand better the underlying mechanisms of protein folding and function, which can lead to the discovery of new drugs or improvements in vaccine development. Furthermore, BAR1’s capacity to express in different host systems facilitates the scaling-up of production for research and commercial purposes. The study of BAR1 also encompasses its interactions with other biomolecules, providing insight into cellular processes and signaling pathways, which are crucial for disease understanding and treatment strategies. Given the growing demand for innovative biopharmaceuticals and sustainable bioprocessing, ongoing research into BAR1 and its derivatives holds promise for addressing critical challenges in health and environmental sectors.
