Analytical Data
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Gene name
EURM2
- Application
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Alternative Names
EURM2；Mite group 2 allergen Eur m 2
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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
Q9TZZ2
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Expression Region
17-145aa
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AA Sequence
DQVDIKDCANHEIKKVMVPGCKGSEPCVIHRGTAFQLEAVFDANQNSNAAKIEIKATIDGVEIDVPGIDNNLCHFMKCPLVKGQEYDIKYTWNVPRIAPKSENVVVTVKLLGDNGVLACAIATHAKIRD
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Molecular Weight
18.1kDa
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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
EURM2 is a recombinant protein that has gained significant attention in the field of biochemistry and molecular biology due to its unique structural and functional properties. Research on EURM2 is driven by its potential applications in various therapeutic and diagnostic contexts, particularly in the treatment of diseases characterized by protein malfunctions. The protein is derived from specific gene sequences and is expressed using advanced biotechnological methods, allowing for the production of large quantities of pure protein. Studies have demonstrated that EURM2 exhibits distinct biochemical functions, such as enzyme catalysis and molecular recognition, which are critical for biological processes. Moreover, understanding the three-dimensional structure of EURM2 can provide insights into its mechanism of action and interaction with other biomolecules. This research is essential not only for basic scientific knowledge but also for the development of novel strategies in drug design and biotechnology. Investigating the stability, activity, and interaction profile of EURM2 may lead to breakthroughs in clinical applications, making it a focal point for ongoing research in related fields.
