Analytical Data
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Gene name
Beta-lactamase TEM/Bla
- Application
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Alternative Names
Carbapenem-hydrolyzing beta-lactamase KPC-2
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Species
Klebsiella oxytoca
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q848S6
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Expression Region
25-293aa
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Molecular Weight
44.5 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
Beta-lactamase TEM (also known as β-lactamase type TEM) is a critical enzyme that provides antibiotic resistance to bacteria, particularly against penicillin and other beta-lactam antibiotics. The emergence of TEM beta-lactamases represents a significant challenge in treating bacterial infections, as these enzymes can hydrolyze a broad spectrum of beta-lactam antibiotics, leading to treatment failure. TEM beta-lactamases are mostly found in Enterobacteriaceae and are often encoded by plasmids, facilitating rapid dissemination among bacterial populations. Research involving the recombinant expression of TEM/Bla proteins is vital for understanding the structure-function relationships of these enzymes, their resistance mechanisms, and the impact of mutations on enzymatic activity. Moreover, studying these proteins in a laboratory setting can inform the development of novel inhibitors and therapeutic strategies to combat antibiotic resistance. This has profound implications for public health, as the increasing prevalence of resistant strains complicates the management of infectious diseases. Therefore, ongoing research into the biochemical properties and genetic variants of TEM beta-lactamases is essential for advancing our knowledge of antibiotic resistance and enhancing the effectiveness of current and future antimicrobial therapies.
