Analytical Data
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Gene name
EGLN2
- Application
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Alternative Names
Estrogen-induced tag 6HPH-3Hypoxia-inducible factor prolyl hydroxylase 1 ;HIF-PH1 ;HIF-prolyl hydroxylase 1 ;HPH-1;Prolyl hydroxylase domain-containing protein 1 ;PHD1
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Species
Human
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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
Q96KS0
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Expression Region
283-407aa
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Molecular Weight
18.1 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
EGLN2, also known as EGLN1-like protein or HIF prolyl hydroxylase 2 (HPH-2), is a critical regulator of the hypoxia-inducible factor (HIF) signaling pathway, which plays a pivotal role in cellular responses to oxygen levels. The study of EGLN2 is driven by its involvement in various physiological and pathological processes, including cancer progression, metabolic adaptation, and ischemic responses. As a member of the EGLN family, EGLN2 hydroxylates specific proline residues on HIF, leading to its degradation under normoxic conditions. In contrast, low oxygen levels inhibit EGLN2 activity, allowing HIF to accumulate and activate target genes involved in angiogenesis, erythropoiesis, and glucose metabolism. Dysregulation of EGLN2 has been implicated in tumor development, where cancer cells exploit the hypoxic response to promote survival and growth in low-oxygen environments. The recombinant production of EGLN2 protein facilitates a deeper understanding of its enzymatic mechanisms, substrate interactions, and regulatory role within the HIF pathway, which is crucial for developing therapeutic strategies aimed at modulating this pathway in diseases like cancer or ischemia. Moreover, the ability to produce active EGLN2 recombinantly allows researchers to perform biochemical assays, drug screenings, and structural studies, further elucidating its function in cellular physiology and pathology. Overall, research on EGLN2 recombinant protein is essential for unlocking new avenues in targeted therapies that could effectively manipulate the HIF signaling axis in various disease contexts.
