Analytical Data
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Gene name
alr2278
- Application
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Alternative Names
alr2278；
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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
Q8YUQ7
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Expression Region
1-189aa
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AA Sequence
MYGLVNKAIQDMISKHHGEDTWEAIKQKAGLEDIDFFVGMEAYSDDVTYHLVGAASEVLGKPAEELLIAFGEYWVTYTSEEGYGELLASAGDSLPEFMENLDNLHARVGLSFPQLRPPAFECQHTSSKSMELHYQSTRCGLAPMVLGLLHGLGKRFQTKVEVTQTAFRETGEDHDIFSIKYEDSNLYDD
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Molecular Weight
65.2 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
ALR2278 is a recombinant protein that has garnered significant interest in recent years due to its potential applications in various fields, including biotechnology and medicine. This protein is derived from a specific bacterial strain known for its ability to produce high yields of recombinant proteins through advanced biotechnological methods. The study of ALR2278 is particularly relevant in the context of protein engineering, where understanding its structure and function can lead to the development of novel therapeutic agents or industrial enzymes. Research has shown that ALR2278 may possess unique biochemical properties, making it an attractive candidate for further investigation in drug development, particularly in targeting diseases where traditional treatment options have proven inadequate. Additionally, the exploration of ALR2278’s interactions with other biomolecules provides insights into its potential role in metabolic pathways, paving the way for innovative approaches in metabolic engineering. As the demand for sustainable and effective bioproducts continues to rise, the study of recombinant proteins like ALR2278 represents a crucial avenue for addressing global health and environmental challenges. Overall, the ongoing research into ALR2278 not only contributes to our understanding of protein function but also holds promise for breakthroughs in therapeutic interventions and biotechnological applications.
