Analytical Data
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Gene name
ampC
- Application
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Alternative Names
ampC；Beta-lactamase
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Species
Human
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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
P24735
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Expression Region
27-397aa
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AA Sequence
GEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR
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Molecular Weight
56.7kDa
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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
AmpC β-lactamase is an important enzyme produced by various Gram-negative bacteria, providing them with resistance to a wide range of beta-lactam antibiotics, including penicillins and cephalosporins. The emergence and dissemination of AmpC-producing strains, especially those that are resistant to third-generation cephalosporins, represent a significant challenge in clinical settings, leading to treatment failures and increased morbidity and mortality. Research on the structure and function of AmpC has been pivotal in understanding its catalytic mechanism and the molecular basis of its β-lactamase activity. Furthermore, studies focusing on the genetic factors that regulate AmpC expression have revealed how environmental pressures, such as antibiotic exposure, can induce AmpC production, thereby contributing to the spread of resistance in bacterial populations. The exploration of AmpC as a therapeutic target is gaining momentum, as novel inhibitors and combination strategies are being evaluated to restore the effectiveness of β-lactam antibiotics against resistant strains. Therefore, the study of AmpC β-lactamase is crucial not only for the development of effective treatment options but also for understanding the broader implications of antibiotic resistance in public health.
