Analytical Data
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Gene name
glmU
- Application
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Alternative Names
glmU；yieA；Bifunctional Protein GlmU
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Species
E.coli
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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
P0ACC7
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Expression Region
1-456aa
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AA Sequence
MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGDLLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADMKRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQSEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKNSVIGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIAAGTTVTRNVGENALAISRVPQTQKEGWRRPVKKK
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Molecular Weight
55.2 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
Related Products
Protein Description
Glucose-6-phosphate dehydrogenase (G6PD) is an essential enzyme involved in the pentose phosphate pathway, playing a crucial role in cellular metabolism and protection against oxidative stress. The glmU gene, which encodes an enzyme involved in the synthesis of the bacterial cell wall component, UDP-GlcNAc, has garnered attention due to its potential as a target for antibiotic development. The glmU protein functions through a bifunctional mechanism, catalyzing two critical reactions: the conversion of fructose-6-phosphate to GlcNAc-6-phosphate and the subsequent conversion to UDP-GlcNAc. Research into the recombinant expression of the glmU protein allows for the in-depth study of its structural and functional properties, as well as its interactions with small molecules, which can lead to the identification of novel inhibitors that may serve as antibiotic agents. Understanding the glmU protein's mechanism and its role in bacterial physiology is vital, especially in the context of rising antibiotic resistance. Consequently, studies focusing on the recombinant production, characterization, and potential applications of the glmU protein represent a significant area of investigation in microbial biochemistry and drug development, with the aim of developing new therapeutic strategies against resistant bacterial strains. By elucidating the biochemical pathways involving glmU, researchers hope to open new avenues for effective treatments and address the global challenge of antibiotic resistance.
