Analytical Data
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Gene name
PHF8
- Application
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Alternative Names
ZNF422; MRXSSD; JHDM1F; Jumonji C Domain-Containing Histone Demethylase 1F; Histone lysine demethylase PHF8
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q80TJ7
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Expression Region
Phe195~Lys351
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Molecular Weight
22kDa
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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
PHF8 (PHD finger protein 8) is a histone demethylase that plays a crucial role in epigenetic regulation by demethylating histone H3 at lysine 9 (H3K9me2) and lysine 27 (H3K27me2), thereby influencing gene expression and cellular processes such as differentiation and proliferation. Given its involvement in various biological processes, PHF8 has garnered significant attention in recent years, particularly in the context of developmental disorders and cancers. Mutations in the PHF8 gene are linked to conditions like Siderius syndrome and intellectual disabilities, highlighting its importance in normal neurodevelopment. Moreover, aberrant expression or dysfunction of PHF8 has been implicated in multiple malignancies, including breast and colorectal cancers, making it a potential biomarker and therapeutic target. The study of PHF8 recombinant proteins provides insights into its biochemical properties, substrate specificity, and mechanisms of action. Understanding the structure-function relationship of PHF8, particularly through the production and characterization of recombinant forms, is essential for elucidating its role in epigenetic regulation and its potential as a target for drug development. Researchers are increasingly employing techniques such as X-ray crystallography and cryo-electron microscopy to reveal the intricate details of PHF8's interactions with histones and other protein partners, which is vital for designing inhibitors or modulators that could have therapeutic benefits in diseases associated with PHF8 dysfunction. The ongoing exploration of PHF8 offers promising avenues in both basic research and clinical applications, underscoring its significance in the field of epigenetics and molecular biology.











