Analytical Data
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Gene name
PFN1
- Application
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Alternative Names
PFN1;Profilin-1
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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
P07737
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Expression Region
2-140aa
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AA Sequence
AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY
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Molecular Weight
41.9kDa
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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
PFN1, or Profilin 1, is a highly conserved actin-binding protein that plays a critical role in cell motility, proliferation, and various signaling pathways. It is essential for the regulation of actin dynamics, influencing cytoskeletal organization, and cellular responses to extracellular signals. Dysregulation of PFN1 can lead to several pathological conditions, including neurodegenerative diseases and cancer. Recent studies have highlighted its involvement in protein-protein interactions and its implications in cellular processes such as gene expression, endocytosis, and organelle transport. Given the importance of PFN1 in maintaining cellular functions, researchers are increasingly focused on understanding its molecular mechanisms and potential as a therapeutic target. Investigations into PFN1 recombinant protein production aim to elucidate its structural and functional properties, providing insight into its role in health and disease. The ability to produce PFN1 in a recombinant form facilitates high-throughput screening and offers a platform for further studies into PFN1-interacting proteins and signaling pathways. This research is crucial for developing targeted therapies that could mitigate PFN1-related diseases by restoring normal cellular function and actin dynamics.
