Analytical Data
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Gene name
SMR3B
- Application
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Species
Human
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Source
HEK293
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Tag
C-mFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NP_006676
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Expression Region
Q23-P79
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Protein Length
Full Length of Mature Protein
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Molecular Weight
35-40 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
The SMR3B protein, a member of the small multi-drug resistance (SMR) family, has drawn significant interest in the field of molecular biology due to its potential role in drug resistance and microbial survival mechanisms. Initially identified in various bacterial species, SMR proteins are known to function as transporters that export toxic compounds, including antibiotics, out of cells, thereby contributing to multidrug resistance. The study of SMR3B is particularly relevant in the context of increasing antibiotic resistance, a pressing global health crisis. Researchers aim to elucidate the structure and function of SMR3B to understand its transport mechanism and substrate specificity. Insights gained from SMR3B could inform the development of novel therapeutic strategies to overcome drug resistance by potentially targeting these transporters. Additionally, the protein's role in cellular stress responses and its involvement in biofilm formation, particularly in pathogenic bacteria, further highlight its significance. Investigating SMR3B not only enhances our understanding of bacterial physiology and pathogenicity but also serves as a critical step toward addressing the challenges posed by antibiotic-resistant infections.
