Analytical Data
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Gene name
EGLN1
- Application
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Alternative Names
EGLN1；C1orf12；Egl nine homolog 1
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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
Q9GZT9
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Expression Region
177-426aa
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AA Sequence
GGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF
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Molecular Weight
35.3 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
EGLN1, also known as prolyl hydroxylase domain-containing protein 2 (PHD2), plays a critical role in the regulation of the hypoxia-inducible factor (HIF) pathway, which is essential for cellular responses to oxygen levels. The enzyme specifically hydroxylates proline residues on HIF-α subunits, leading to their subsequent degradation under normoxic conditions. In contrast, during hypoxia, EGLN1 activity is inhibited, allowing HIF-α to accumulate and activate genes that facilitate adaptive responses such as erythropoiesis, angiogenesis, and metabolic adjustments. Research into EGLN1 recombinant protein has gained momentum due to its potential implications in various physiological and pathological contexts, including cancer, ischemic diseases, and metabolic disorders. By producing and characterizing EGLN1 as a recombinant protein, scientists aim to better understand its enzymatic mechanisms, regulation, and interaction with other cellular components. Furthermore, insights gained from EGLN1 research may pave the way for the development of novel therapeutic strategies targeting hypoxia-related conditions, offering promising avenues in regenerative medicine and oncology. Overall, studying EGLN1 not only elucidates fundamental biological processes but also holds significant promise for innovative treatment approaches in diseases where oxygen sensing and response are disrupted.
