Analytical Data
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Gene name
LACTb
- Application
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Alternative Names
G24; MRPL56; Mitochondrial Ribosomal Protein L56; Serine beta-lactamase-like protein LACTB, mitochondrial
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P83111
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Expression Region
Leu313~Asp547
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Molecular Weight
30kDa
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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
LACTB (lactamase beta) is an important protein that plays a crucial role in bacterial resistance and metabolism. Discovered as a part of the bacterial enzyme family, LACTB has been implicated in the hydrolysis of beta-lactam antibiotics, which are essential in treating a variety of bacterial infections. The emergence of antibiotic resistance poses a significant threat to public health, making the study of LACTB particularly relevant. Research has shown that LACTB can not only confer resistance to antibiotics but also participate in other cellular processes, such as cell signaling and apoptosis. Recent studies have focused on the structural and functional characterization of LACTB, utilizing recombinant protein techniques to produce and purify the enzyme for in-depth analysis. Understanding LACTB's mechanism of action and its interactions with other cellular components could pave the way for developing novel therapeutic strategies to combat antibiotic-resistant bacteria. Additionally, exploring LACTB's role in metabolic pathways offers insights into its potential functions beyond antibiotic resistance. Overall, the research on LACTB is significant in addressing the global challenge of antibiotic resistance and advancing our knowledge of bacterial biology.
