Analytical Data
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基因名
P4HTM
- Application
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别名
Hypoxia-inducible factor prolyl hydroxylase 4 ;HIF-PH4 ;HIF-prolyl hydroxylase 4 ;HPH-4
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9NXG6
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表达区间
82-563aa
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分子量
70.5 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.
Quality inspection process
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Protein Description
P4HTM (Prolyl 4-Hydroxylase-Tryptophan Mutase) is an enzyme known for its pivotal role in post-translational modification processes, particularly in the hydroxylation of proline residues in various proteins. This process is essential for stabilizing collagen triple helices, thus directly influencing tissue integrity and function. The significance of P4HTM extends beyond collagen synthesis; it is also implicated in the regulation of hypoxia-inducible factors (HIFs), which play crucial roles in cellular responses to oxygen levels. Given its involvement in these fundamental biological processes, abnormalities in P4HTM activity have been linked to several diseases, including cardiovascular disorders, fibrosis, and various cancers. Recent research has focused on understanding the molecular mechanisms of P4HTM, exploring its potential as a therapeutic target. Advances in recombinant protein technology have enabled the production of P4HTM variants for detailed structural and functional studies, paving the way for novel therapeutic strategies and biomarker development. With ongoing investigations into its enzymatic properties and interactions with other biological molecules, P4HTM remains a compelling subject in the fields of biochemistry and molecular biology, highlighting its relevance in health and disease.
