Analytical Data
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Gene name
murI
- Application
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Alternative Names
murI; HPG27_509; Glutamate racemase; EC 5.1.1.3
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Species
Helicobacter pylori
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
B5Z6S2
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Expression Region
1-255aa
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Molecular Weight
35.9 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
MurI, or Murein hydrolase inhibitor, is a protein that plays a critical role in bacterial cell wall synthesis and maintenance. Research on MurI has gained prominence due to its potential as a target for novel antibiotic development, amidst the global challenge of antibiotic resistance. This protein acts as an inhibitor of murein hydrolases, enzymes that are essential for breaking down the peptidoglycan layer of bacterial cell walls during cell division and growth. By inhibiting these enzymes, MurI contributes to the stability and integrity of the bacterial cell wall, allowing for potential virulence in pathogenic bacteria. Given the rising incidence of antibiotic-resistant strains such as MRSA (Methicillin-resistant Staphylococcus aureus) and others, understanding MurI's structure, function, and mechanisms of action is crucial for developing new therapeutic strategies. Additionally, research has shown that MurI is involved in the regulation of the bacterial cell cycle and may interact with various cellular pathways, indicating its multifaceted role in bacterial physiology. Consequently, studies focusing on MurI can provide insights into not only bacterial survival mechanisms but also pathways that can be exploited for drug discovery, highlighting its significance in the field of microbiology and antibiotic research. The exploration of MurI and its interactions could lead to innovative approaches to combat bacterial infections that are resistant to current antibiotics, underscoring its importance in addressing public health challenges associated with antimicrobial resistance.
