Analytical Data
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Gene name
E53A
- Application
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Alternative Names
1,4-beta-N-acetylmuramidase C;Allergen Gal d IV;Gal d 4
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Species
Chicken
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00698
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Expression Region
19-147aa
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Molecular Weight
14.4 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
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Protein Description
The E53A recombinant protein has garnered significant attention in the field of molecular biology and biochemistry due to its unique structure and potential applications. E53A is a variant of a protein that is derived from a specific organism, often utilized in studies aimed at understanding protein function, interaction, and stability. Research surrounding this protein focuses on its role in various biological processes, including cell signaling, immune response, and disease progression. The E53A mutation, which involves a single amino acid substitution, is hypothesized to impact the protein's stability and activity, making it an ideal candidate for investigating structure-function relationships. Additionally, this protein's relevance extends to drug discovery and therapeutic interventions, given its potential as a biomarker or target for novel treatments. The characterization of E53A not only contributes to the fundamental knowledge of protein dynamics but also paves the way for innovative strategies in biotechnology and medicine. As research progresses, the insights gained from E53A studies are expected to enhance our understanding of complex biological systems and foster advancements in therapeutic development.
