Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Study indicated that PFN2 may function as a negative regulator of colorectal cancer (CRC) metastasis and, thus, may represent a potential target for CRC therapy.
High PFN2 expression might serve as a valuable predictor for poor overall survival of HNSC. DNA amplification and hypomethylation might be two mechanisms of PFN2 dysregulation.
PFN2 gene, related to regulation of actin cytoskeleton in protein complex F, might play momentous roles in the initiation and development of consecutive Trauma-Induced Sepsis.
PFN2 has a novel role in promoting Esophageal squamous cell carcinoma progression and metastasis.
Data suggest 2 major isoforms of profilin (Pfn1 and Pfn2) are co-regulated by a common mechanism involving the action of MKL1 [megakaryoblastic leukemia (translocation) 1 protein] that is independent of its SRF- (serum-response factor)-related activity; cellular externalization of Pfn1, rather than transcription, is affected by the perturbations of MKL1; MKL1 can influence cell migration by modulating Pfn1 expression.
Study demonstrated that miR30a inhibits epithelial-mesenchymal transition (EMT) and invasion in highly invasive non-small cell lung cancer (NSCLC) cell lines via targeting PFN2 suggesting that miR30a with PFN2 may play an essential role in the development of NSCLC by modulating EMT and cell invasion.
Disease causing mutations in inverted formin 2 regulate its binding to G-actin, F-actin capping protein (CapZ alpha-1) and profilin 2.
Therefore, this study indicates that profilin 2 affects the metastatic potential and stemness of colorectal CSCs by regulating EMT- and stemness-related proteins.
Pfn2 suppresses the recruitment of HDAC1 to Smad2 and Smad3 promoters, increasing their expression, and, in turn, enhancing TGFB1 induced epithelial-mesenchymal transformation and VEGF and CTGF production.
effects of profilin-1 and profilin-2, the two major isoforms of profilin, on actin cytoskeletal regulation, motility, and invasion of breast cancer cells
Oral squamous cell carcinomas with weak PFN2 expression were associated with a significantly worse prognosis than strongly expressed tumours.
These findings raise the possibility that Rgl3 mediates interaction between Ras/Rap-family proteins and profilin II, an important activator of actin polymerization.
A signaling pathway from ROCK1 to profilin controls polyglutamine protein aggregation.
RARalpha competes with other PFN2a-binding proteins bearing PRMs and involved in actin filaments elongation. Consequently, the actin filament network is altered and MEFs adhesion is decreased. This novel role opens novel avenues for the understanding of pathologies characterized by increased levels of cytoplasmic RARalpha.
Pfn2 expression is controlled by the iron regulatory proteins in vivo and that Pfn2 contributes to maintaining iron homeostasis in cell lines and mice.
knockdown of profilin 1 or profilin 2a led to significant decrease in cell spreading of astrocytes. the knockdown of profilin 2a resulted in a significantly reduced morphological complexity of astrocytes in both dissociated and slice culture astrocytes.
Hyper-phosphorylation of profilin2a is the molecular link between SMN and the ROCK pathway repressing neurite outgrowth in neuronal cells.
Profilin II regulates the exocytosis of kainate glutamate receptors.
Phosphatidylinositol 4,5-bisphosphate releases Pfn2 from the Pfn2-dynamin 1 complex as well as from the Pfn2-actin complex, suggesting that Pfn2 is diverging the phosphoinositide signaling pathway to actin polymerization as well as endocytosis
Following NMDA receptor activation profilin 2 accumulates not only in dendritic spines, but also in the nucleus of hippocampal neurons via a process involving rearrangement of the actin cytoskeleton.
results highlight a novel, profilin2-dependent pathway, regulating synaptic physiology, neuronal excitability, and complex behavior
High-resolution structural analysis of mouse profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP.
Upregulation of profilin 2 by BFA was verified by immunoblot and live imaging at subcellular level.
localized to polygonal meshes resembling the endoplasmic reticulum
The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. There are two alternatively spliced transcript variants encoding different isoforms described for this gene.
, profilin 2