Analytical Data
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Gene name
PFN2
- Application
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Alternative Names
PFL
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Species
Human
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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
P35080
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Expression Region
Gln5~Phe140
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Molecular Weight
18kDa
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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
PFN2 (Profilin 2) is a member of the profilin family of actin-binding proteins, which play a crucial role in regulating actin cytoskeleton dynamics and cellular processes such as cell motility, division, and shape maintenance. The study of PFN2 has garnered interest due to its potential implications in various physiological and pathological conditions, including cancer, neurodegenerative diseases, and muscle disorders. Recent research has highlighted PFN2's role in modulating the actin polymerization process and interaction with other actin-associated proteins, suggesting that it could be a key player in orchestrating cellular responses to environmental cues. Furthermore, abnormal expression levels of PFN2 have been associated with tumor progression and metastasis, indicating that it might serve as a therapeutic target. Advances in recombinant protein technology have enabled the production of PFN2, allowing for in-depth functional assays and structural studies. This research aims to elucidate the molecular mechanisms underlying PFN2's actions, providing insights that could lead to innovative treatments for diseases linked to actin dysregulation. Understanding the structure-function relationship of PFN2 through recombinant protein studies can unveil novel strategies for modulating its activity, thereby influencing actin dynamics and contributing to cancer therapy or regenerative medicine efforts.
