Analytical Data
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Gene name
mrcA
- Application
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Alternative Names
mrcA；ponA；Penicillin-binding Protein 1A
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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
P02918
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Expression Region
229-529aa
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AA Sequence
MLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQQATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLAQVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVM
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Molecular Weight
81.2 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
MrcA (Murein hydrolase-associated protein A) is a significant protein involved in bacterial cell wall metabolism, particularly in the context of antibiotic resistance and peptidoglycan synthesis. The study of MrcA has gained attention due to its role in the structural integrity of bacterial cells and its potential as a target for novel antimicrobial therapies. As antibiotic resistance becomes an escalating global health concern, understanding the mechanisms of MrcA and its function in bacterial cell wall remodeling is crucial. Research indicates that MrcA may participate in the hydrolysis of peptidoglycan, facilitating bacterial growth and division. Structural and functional analyses of MrcA could reveal unique binding sites or enzymatic activities that can be exploited for drug development. Additionally, investigating the genetic regulation and expression profiles of MrcA across different bacterial species may shed light on its evolutionary adaptations and its varying contributions to virulence and resistance. The exploration of MrcA's role in bacterial physiology not only enhances our understanding of fundamental biological processes but also opens avenues for innovative strategies to combat resistant strains of bacteria.
