Analytical Data
-
Gene name
PFN4
- Application
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NHR9
-
Expression Region
Met1~Arg125
-
Molecular Weight
17.6kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PFN4, or Profilin 4, is a member of the profilin family of actin-binding proteins, which play a crucial role in regulating the dynamics of the actin cytoskeleton. The interest in studying PFN4 has surged due to its potential involvement in various cellular processes, such as cell migration, proliferation, and differentiation. Research has indicated that PFN4 is differentially expressed in various tissues, suggesting that it may have tissue-specific functions. Furthermore, increasing evidence highlights its potential role in several pathological conditions, including cancer and neurodegenerative diseases, by contributing to altered cellular morphology and motility. Understanding the molecular mechanisms by which PFN4 regulates these processes may provide insights into the underlying causes of these diseases and open avenues for therapeutic interventions. Consequently, the recombinant expression and purification of PFN4 have become essential for characterizing its biochemical properties and interactions with other cellular components. This research not only aims to elucidate the functional aspects of PFN4 but also to explore its potential as a biomarker or therapeutic target in relevant diseases, presenting exciting prospects for future studies in cell biology and medicine.
