Analytical Data
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Gene name
AMR
- Application
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Alternative Names
AMR；Nuclear Protein AMMECR1
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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
Q9Y4X0
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Expression Region
1-333aa
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AA Sequence
MAAGCCGVKKQKLSSSPPSGSGGGGGASSSSHCSGESQCRAGELGLGGAGTRLNGLGGLTGGGSGSGCTLSPPQGCGGGGGGIALSPPPSCGVGTLLSTPAAATSSSPSSSSAASSSSPGSRKMVVSAEMCCFCFDVLYCHLYGYQQPRTPRFTNEPYPLFVTWKIGRDKRLRGCIGTFSAMNLHSGLREYTLTSALKDSRFPPMTRDELPRLFCSVSLLTNFEDVCDYLDWEVGVHGIRIEFINEKGSKRTATYLPEVAKEQGWDHIQTIDSLLRKGGYKAPITNEFRKTIKLTRYRSEKMTLSYAEYLAHRQHHHFQNGIGHPLPPYNHYS
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Molecular Weight
35.4 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
AMR (Antimicrobial Resistance) has emerged as a critical global health challenge, significantly impacting treatment options for bacterial infections. Research into recombinant proteins associated with AMR aims to understand the mechanisms of resistance and develop novel therapeutic strategies. Bacteria can acquire resistance through various means, including horizontal gene transfer and mutations, leading to the production of enzymes like beta-lactamases, which degrade antibiotics. The study of AMR recombinant proteins involves the genetic engineering of bacteria to produce these proteins in a controlled laboratory setting, allowing researchers to analyze their structure and function. This approach not only enhances the understanding of how these proteins confer resistance but also aids in the development of inhibitors that can combat resistant strains. The research encompasses various bacterial species, focusing on both Gram-positive and Gram-negative bacteria, to encompass a broad spectrum of AMR determinants. Furthermore, recombinant proteins can serve as potential candidates for novel vaccines or therapeutic agents, contributing to the ongoing battle against AMR by providing new avenues for treatment. The urgency of addressing AMR is underscored by increasing rates of infection, prolonged hospital stays, and higher healthcare costs, motivating interdisciplinary research efforts in microbiology, biochemistry, and pharmacology to effectively tackle this pressing public health issue.
