Analytical Data
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Gene name
Egln3
- Application
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Alternative Names
Hypoxia-inducible factor prolyl hydroxylase 3 ;HIF-PH3 ;HIF-prolyl hydroxylase 3 ;HPH-3;Prolyl hydroxylase domain-containing protein 3 ;PHD3SM-20
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Species
Mouse
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q91UZ4
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Expression Region
2-239aa
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Molecular Weight
31.2 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
EGLN3, also known as Egl-9 family hypoxia-inducible factor 3, is a member of the EGLN (Egl-9 family of proteins) family that plays a crucial role in the cellular response to hypoxia. This protein functions as a prolyl hydroxylase, which regulates the stability and activity of hypoxia-inducible factors (HIFs) by hydroxylating specific proline residues. In normoxic conditions, EGLN3 mediates the degradation of HIFs, preventing the transcription of genes that facilitate adaptation to low oxygen levels. Conversely, under hypoxic conditions, EGLN3 activity decreases, allowing for the stabilization and accumulation of HIFs, which in turn activate a range of genes involved in angiogenesis, erythropoiesis, and metabolic adaptation. Research on recombinant EGLN3 protein has gained importance due to its potential implications in understanding various physiological and pathological processes, including cancer biology, where tumor cells often exploit hypoxic pathways for survival and growth. Moreover, the modulation of EGLN3 activity is being explored as a therapeutic strategy in diseases characterized by inadequate oxygen supply, such as ischemic conditions and certain genetic disorders. The study of recombinant EGLN3 not only enhances our understanding of its enzymatic mechanisms but also paves the way for the development of novel interventions targeting hypoxic responses in diverse diseases. Thus, the investigation of EGLN3 recombinant protein is pivotal for advancing our knowledge of hypoxia-related biology and for the potential development of innovative therapeutic strategies.
