Analytical Data
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Gene name
tetM
- Application
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Alternative Names
tetA(M)
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Species
Staphylococcus aureus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q53770
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Expression Region
1-242aa
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Molecular Weight
32.1 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
TetM is a ribosomal protection protein that confers resistance to tetracycline, one of the most widely used antibiotics. It is primarily found in various Gram-positive bacteria, particularly those in the genus *Enterococcus*. The increasing prevalence of antibiotic resistance, especially among pathogenic bacteria, has raised significant concerns in the medical community. Understanding the mechanisms behind tetM gene expression and function is crucial for developing strategies to combat antibiotic resistance. Research has focused on the molecular characteristics of tetM, including its role in ribosome protection and its potential as a target for novel therapeutic interventions. Recent studies have investigated the structural basis of TetM's interaction with the ribosome, revealing insights into how it displaces tetracycline from the ribosomal RNA binding sites, thus allowing protein synthesis to continue despite the presence of the antibiotic. This research not only enhances our comprehension of bacterial resistance mechanisms but also guides the development of new antibiotics or adjuvants that could restore the efficacy of tetracyclines against resistant strains. As antibiotic resistance continues to pose a significant threat to public health, the study of TetM and other resistance mechanisms remains a critical area of investigation in microbiology and pharmacology.
