Analytical Data
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Gene name
PHF5A
- Application
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Alternative Names
PHF5A;PHD finger-like domain-containing Protein 5A
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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
Q7RTV0
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Expression Region
1-110aa
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AA Sequence
MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
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Molecular Weight
39.4kDa
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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
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Protein Description
PHF5A (PHD finger protein 5A) is a protein that belongs to the PHD (Plant Homeodomain) finger family, which is known for its involvement in various biological processes, including gene regulation, epigenetic modifications, and chromatin remodeling. Recent studies have highlighted the role of PHF5A in several cellular functions, including cell proliferation, differentiation, and response to stress. Its expression levels have been implicated in multiple diseases, particularly cancer, suggesting that PHF5A may function as an oncogene or tumor suppressor depending on the context. Research into PHF5A has accelerated due to its potential as a biomarker for specific cancers and its role in the regulation of splicing factors, which are critical for mRNA processing. Additionally, the development of recombinant PHF5A protein has enabled scientists to investigate its biochemical properties and interactions with other cellular components. Understanding the functional dynamics of PHF5A at a molecular level could provide insights into its role in disease mechanisms and open new avenues for therapeutic interventions. These research endeavors aim to elucidate the significance of PHF5A in cellular processes and how its dysregulation may contribute to various pathological conditions, thereby underscoring the importance of continued investigation into this multifaceted protein.
