Analytical Data
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Gene name
P4HTM
- Application
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Alternative Names
Hypoxia-inducible factor prolyl hydroxylase 4 ;HIF-PH4 ;HIF-prolyl hydroxylase 4 ;HPH-4
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NXG6
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Expression Region
82-563aa
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Molecular Weight
70.5 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
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.
