Analytical Data
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Gene name
ELOA3DP
- Application
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Species
Human
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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
A6NLF2
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Expression Region
270-429aa
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Molecular Weight
25.9 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
ELOA3DP, a protein derived from the ELOA gene family, has garnered significant attention in the field of molecular biology and biochemistry due to its unique structural characteristics and functional properties. Originally identified in studies focused on alternative splicing and post-translational modifications, ELOA3DP has been implicated in various physiological processes, including cell signaling, metabolism, and developmental regulation. Research has revealed that the restructured form of ELOA3DP exhibits enhanced stability and bioactivity, making it a promising candidate for therapeutic applications, particularly in regenerative medicine and disease models. The understanding of its molecular interactions and mechanisms of action has opened new avenues for targeting specific pathways involved in cellular dysfunctions. Furthermore, with the advancement of techniques such as CRISPR/Cas9 genome editing and protein engineering, researchers are now able to manipulate and study ELOA3DP with greater precision, paving the way for innovative strategies in drug design and therapeutic interventions. This growing body of research emphasizes the importance of ELOA3DP in the broader context of protein science and its potential impact on health and disease management, warranting further exploration and characterization of this innovative protein.
