Analytical Data
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Gene name
msyB
- Application
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Alternative Names
msyB；Acidic Protein MsyB
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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
1-124aa
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Expression Region
1-124aa
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AA Sequence
MTMYATLEEAIDAAREEFLADNPGIDAEDANVQQFNAQKYVLQDGDIMWQVEFFADEGEEGECLPMLSGEAAQSVFDGDYDEIEIRQEWQEENTLHEWDEGEFQLEPPLDTEEGRAAADEWDER
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Molecular Weight
16.3 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
Related Products
Protein Description
MsbY is a membrane-bound protein that plays a crucial role in the transport of lipid A, a component of lipopolysaccharides found in the outer membrane of Gram-negative bacteria. Research into MsB has garnered significant attention in the context of antibiotic resistance and bacterial virulence, as it is implicated in the assembly and translocation of lipopolysaccharides, which are essential for bacterial integrity and immune evasion. Understanding the structure and function of MsB and its interactions at the molecular level is vital for developing new therapeutic strategies against Gram-negative bacterial infections, especially given the rising prevalence of multidrug-resistant strains. Recombinant MsbY proteins are often produced for biochemical and structural studies, allowing researchers to elucidate the protein’s function and its role in bacterial physiology. Additionally, these studies can highlight potential targets for novel antibiotic development, aiming to disrupt the function of MsB and thereby weaken bacterial defenses. Consequently, the investigation of MsbY not only enhances our understanding of bacterial biology but also contributes to the ongoing battle against antibiotic resistance in a clinical setting.
