Analytical Data
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Gene name
PHF5A
- Application
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Alternative Names
Splicing factor 3B-associated 14KDA protein ;SF3b14b
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Species
Human
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Source
E. coli
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Tag
N- GST
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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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Molecular Weight
39.4 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
PHF5A (PHD Finger Protein 5A) is a member of the PHD finger protein family, which are characterized by the presence of a PHD finger motif involved in protein-protein and protein-DNA interactions. The function of PHF5A has garnered attention due to its potential roles in various biological processes, including gene regulation, cell differentiation, and development. Recent studies have indicated that PHF5A may be implicated in certain cancers and diseases, suggesting that it might be a critical player in cellular signaling pathways. The investigation of recombinant PHF5A proteins has become essential for elucidating its structure-function relationships, and its interactions with other cellular components. By producing recombinant PHF5A in suitable expression systems, researchers aim to produce sufficient quantities of the protein for both biochemical characterization and functional studies. Understanding the precise mechanisms by which PHF5A operates can provide insights into its biological roles and therapeutic potential, especially in the context of diseases where its expression or function may be altered. Therefore, research on PHF5A recombinant proteins not only enhances our understanding of this protein’s fundamental biology but also opens up avenues for developing potential interventions in disease states linked to abnormal PHF5A activity.
