Analytical Data
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Gene name
Profilin-4
- Application
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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 95% as determined by SDS-PAGE.
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Uniprot
Q9D6I3
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Expression Region
Met1~Arg125
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Molecular Weight
17.7kDa
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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
Profilin-4, a member of the profilin family of actin-binding proteins, has garnered significant attention due to its potential roles in cellular processes such as cytoskeletal reorganization, signal transduction, and membrane dynamics. It is predominantly expressed in the brain and has been implicated in various neurological functions and diseases, including neurodevelopmental disorders and neurodegeneration. Recent studies have suggested that Profilin-4 may interact with specific cellular signaling pathways and cytoskeletal elements, influencing neuronal morphology and function. The investigation of recombinant Profilin-4 protein has provided insights into its biophysical properties and functional mechanisms at the molecular level. Researchers have utilized recombinant techniques to produce Profilin-4 for in vitro analyses, focusing on its binding affinities, structural characteristics, and interactions with other proteins, such as phosphoinositides and small GTPases. Understanding these interactions is crucial for elucidating the role of Profilin-4 in health and disease, paving the way for potential therapeutic interventions aimed at modulating its function in neurological contexts. The ongoing research into Profilin-4 not only deepens our understanding of actin dynamics but also holds promise for developing strategies to address disorders linked to its dysregulation.
