Analytical Data
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Gene name
ELANE
- Application
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Alternative Names
ELANE;ELA2;Neutrophil elastase
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Species
Human
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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
P08246
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Expression Region
30-267aa
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AA Sequence
IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH
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Molecular Weight
25.7 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
ELANE, or elastase, is an enzyme primarily produced by neutrophils and plays a crucial role in the immune response by degrading extracellular matrix components and modulating inflammation. Dysfunctional ELANE is linked to various pathological conditions, including congenital neutropenia and chronic inflammatory diseases. Research on recombinant ELANE proteins has gained momentum in recent years due to their potential therapeutic applications. By producing ELANE in a recombinant form, researchers can study its structure-function relationships, mechanisms of action, and the effects of specific mutations that could influence its activity. Additionally, recombinant ELANE can be engineered for enhanced stability, specificity, and efficacy in clinical applications. Such advancements could pave the way for new treatments aimed at restoring normal immune function in patients suffering from ELANE-related disorders or for developing novel therapeutics that harness the enzyme’s properties to target pathological processes effectively. Overall, the study of recombinant ELANE holds promise not only for understanding its biological significance but also for translating these insights into innovative therapeutic strategies.











