关键信息
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基因名
Egln3
- 应用
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别名
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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种属
Mouse
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q91UZ4
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表达区间
2-239aa
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分子量
31.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
质检流程
相关产品
背景信息
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.
