Analytical Data
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Gene name
EGLN3
- Application
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Alternative Names
EGLN3;Prolyl hydroxylase EGLN3
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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
Q9H6Z9
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Expression Region
1-239aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED
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Molecular Weight
30 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
Related Products
Protein Description
EGLN3, also known as Egl-nine homolog 3, plays a critical role in the regulation of oxygen homeostasis and is involved in the cellular response to hypoxia through its function as a prolyl hydroxylase. It is part of the larger EGLN family, which facilitates the hydroxylation of hypoxia-inducible factors (HIFs), thereby influencing their stability and activity under varying oxygen levels. Research has indicated that EGLN3 may have implications in various biological processes, including angiogenesis, metabolism, and the progression of certain diseases such as cancer. Given its regulatory role in HIF pathways, EGLN3 has emerged as a potential therapeutic target for conditions characterized by aberrant hypoxic responses. The study of recombinant EGLN3 proteins is crucial for understanding its biochemical properties, structure-function relationships, and interaction with substrates. Furthermore, recombinant protein studies can help elucidate the enzyme's role in different physiological and pathological conditions, paving the way for innovative approaches in drug design and therapy, particularly in combating diseases with hypoxia-related mechanisms.
