Analytical Data
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Gene name
EGLN2
- Application
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Alternative Names
EGLN2；EIT6；Prolyl hydroxylase EGLN2
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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
Q96KS0
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Expression Region
283-407aa
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AA Sequence
MVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT
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Molecular Weight
32.3 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 Egl-9 family hypoxia-inducible factor 2, plays a crucial role in cellular responses to hypoxia by regulating the stability of hypoxia-inducible factors (HIFs). As an important oxygen-sensing enzyme, EGLN2 belongs to the prolyl hydroxylase domain (PHD) family and is primarily involved in the post-translational modification of HIF-α subunits, facilitating their degradation under normoxic conditions. When oxygen levels are low, EGLN2 activity decreases, leading to the stabilization and accumulation of HIFs, which then activate numerous genes involved in adaptive responses such as angiogenesis, erythropoiesis, and metabolism. Research on EGLN2 recombinant protein has gained traction due to its potential implications in various pathophysiological conditions, including cancer, ischemic diseases, and metabolic disorders. Understanding the structure and function of EGLN2 through recombinant protein studies provides insights into its catalytic mechanism and interaction with HIFs, which could aid in the development of targeted therapies that manipulate the hypoxic response. Furthermore, due to its role in tumor progression and metastasis, EGLN2 is being explored as a possible therapeutic target for cancer treatment. Overall, the study of EGLN2 recombinant protein not only enhances our comprehension of hypoxic signaling pathways but also opens up avenues for innovative interventions in diseases associated with dysregulated oxygen homeostasis.
