Analytical Data
-
Gene name
PFN2
- Application
-
Alternative Names
PFN2;Profilin-2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P35080
-
Expression Region
1-140aa
-
AA Sequence
MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPIEIDM IVGKDREGFFTNGLALGAKKCSVIRDSLYVDGDCTMDIRTKSQGGEPTYN VAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF
-
Molecular Weight
15 kDa
-
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
PFN2, or profilin 2, is a multifunctional actin-binding protein that plays a critical role in cytoskeletal dynamics, cell motility, and various cellular processes. Its involvement in the regulation of actin polymerization has garnered attention, particularly in the context of neuronal development and synaptic function. PFN2 is highly expressed in the brain, suggesting a crucial role in neuronal processes such as growth cone dynamics and the formation of dendritic spines, which are essential for synaptic plasticity and learning. Aberrant expression or dysfunction of PFN2 has been implicated in several neurodegenerative diseases and cancers, highlighting its potential as a therapeutic target. Recent studies utilizing recombinant PFN2 protein have aimed to elucidate its structural and functional properties, providing insights into its mechanisms of action at the molecular level. By investigating the interactions of PFN2 with various actin-associated proteins and its role in signaling pathways, researchers hope to develop strategies for modulating its function in disease contexts. Furthermore, understanding PFN2’s role in cellular processes may open avenues for innovative therapeutic approaches in treating diseases characterized by dysregulated actin dynamics. Thus, the study of recombinant PFN2 protein continues to be a vital area of research within cellular and molecular biology.
