Analytical Data
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Gene name
MEP1a
- Application
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Alternative Names
MEP1A;Meprin A subunit alpha
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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
Q16819
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Expression Region
22-601aa
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AA Sequence
ADPVPIKYLPEENVHDADFGEQKDISEINLAAGLDLFQGDILLQKSRNGL RDPNTRWTFPIPYILADNLGLNAKGAILYAFEMFRLKSCVDFKPYEGESS YIIFQQFDGCWSEVGDQHVGQNISIGQGCAYKAIIEHEILHALGFYHEQS RTDRDDYVNIWWDQILSGYQHNFDTYDDSLITDLNTPYDYESLMHYQPFS FNKNASVPTITAKIPEFNSIIGQRLDFSAIDLERLNRMYNCTTTHTLLDH CTFEKANICGMIQGTRDDTDWAHQDSAQAGEVDHTLLGQCTGAGYFMQFS TSSGSAEEAALLESRILYPKRKQQCLQFFYKMTGSPSDRLVVWVRRDDST GNVRKLVKVQTFQGDDDHNWKIAHVVLKEEQKFRYLFQGTKGDPQNSTGG IYLDDITLTETPCPTGVWTVRNFSQVLENTSKGDKLQSPRFYNSEGYGFG VTLYPNSRESSGYLRLAFHVCSGENDAILEWPVENRQVIITILDQEPDVR NRMSSSMVFTTSKSHTSPAINDTVIWDRPSRVGTYHTDCNCFRSIDLGWS GFISHQMLKRRSFLKNDDLIIFVDFEDITHLSQHHHHHH
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Molecular Weight
67 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
MEP1a, a member of the metallo-β-lactamase (MBL) family, has garnered significant interest in the field of biochemistry and molecular biology due to its potential implications in antibiotic resistance and therapeutic development. As bacteria continue to evolve mechanisms to resist beta-lactam antibiotics—one of the most commonly used classes in clinical settings—understanding the structure and function of MEP1a becomes critical. This protein exhibits unique enzymatic activity that allows it to hydrolyze various beta-lactam compounds, rendering them ineffective. Research has focused on the recombinant expression of MEP1a to facilitate detailed investigations into its biochemical properties, substrate specificity, and catalytic mechanisms. By employing advanced techniques such as site-directed mutagenesis and X-ray crystallography, scientists aim to elucidate the molecular basis of MEP1a's function and its interaction with inhibitors. This knowledge could inform the design of novel therapeutics targeting MBLs, contributing to the ongoing battle against multidrug-resistant bacterial infections. Additionally, studying MEP1a's evolutionary adaptations may provide insights into the broader mechanisms of antibiotic resistance, ultimately leading to the development of more effective treatment strategies.
