Analytical Data
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Gene name
mscL
- Application
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Alternative Names
mscL;Scl;Selenocysteine lyase
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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
P0A743
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Expression Region
1-136aa
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AA Sequence
MSIIKEFREFAMRGNVVDLAVGVIIGAAFGKIVSSLVADIIMPPLGLLIGGIDFKQFAVTLRDAQGDIPAVVMHYGVFIQNVFDFLIVAFAIFMAIKLINKLNRKKEEPAAAPAPTKEEVLLTEIRDLLKEQNNRS
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Molecular Weight
29.0 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
MscL (Mechanosensitive Channel of Large Conductance) is a vital protein that plays a crucial role in bacterial osmoregulation by providing a pathway for ions and small molecules to traverse the cell membrane in response to mechanical stress. Understanding MscL is essential due to its implications in cellular stress responses and its potential as a target for antibiotic development. The protein itself is a homopentameric channel that opens under high tension, allowing for the rapid release of solutes to prevent cellular lysis. Research on MscL has advanced significantly with the advent of recombinant protein technology, enabling the production of large quantities of purified MscL for structural and functional studies. Methods such as X-ray crystallography and cryo-electron microscopy have yielded insights into its structural conformation and gating mechanism. These studies not only illuminate the fundamental principles of mechanosensation in bacteria but also pave the way for biotechnological applications. The ability to incorporate MscL into synthetic membranes or study its interactions with various lipid environments enhances our understanding of membrane biology and could lead to innovative approaches in biomimetic materials. Furthermore, the investigation of MscL's channel properties, ion selectivity, and its response to mechanical stimuli remains a vibrant area of research with implications in fields ranging from microbiology to biophysics and pharmaceuticals. Overall, the exploration of recombinant MscL is pivotal for unraveling the complexities of mechanotransduction and facilitating advances in bioscience.











