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anti-Human Formin 2 Anticorps:
anti-Mouse (Murine) Formin 2 Anticorps:
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Human Polyclonal Formin 2 Primary Antibody pour ELISA, WB - ABIN566042
Belin, Lee, Mullins: DNA damage induces nuclear actin filament assembly by Formin-2 and Spire-½ that promotes efficient DNA repair. dans eLife 2015
FMN2 promoter hypermethylation may be an important early event in colorectal cancer, most likely playing a critical role in cancer initiation, and can serve as an ideal diagnostic biomarker in elderly patients with early-stage colon cancer.
Overexpressing FMN2 reversed the inhibitory effects of miR-144-upregulation on acute lymphoblastic leukemia proliferation and cell-cycle transition
Fmn2 mutant mice develop accelerated age-associated memory decline that is further increased in the presence of additional risk factors and is mechanistically linked to a loss of transcriptional homeostasis.
This DNA damage-induced nuclear actin assembly requires two biologically and physically linked nucleation factors: Formin-2 and Spire-1/Spire-2.
We therefore characterized co-expressed Spir-2 and Fmn-2 fluorescent protein fusions . The data corroborate a model according to which Spir-2 exists in two different states, a cytosolic monomeric conformation and a membrane-bound state
FMN2 mutations link intellectual disability either directly or indirectly to the regulation of actin-mediated synaptic spine density.
miR-335 regulates the expression of at least five formin family members, three of which are validated, FMNL3, FMN2 and DAAM2.
FMN2 is a crucial protein involved in the control of p21.
results identify FMN2 as a crucial component in the regulation of p21 and consequent oncogene/stress-induced cell-cycle arrest in human cells.
analysis of the molecular basis of the Spir1/formin-2 interaction
FMN2 was characterized at human chromosome 1q43.
It is likely that FMN2 has the same function as Fmn2 in the mouse, i.e., maintenance of the meiotic spindle. Identification of patients with meiosis I arrest is necessary to determine whether FMN2 mutations are a cause of unexplained infertility.
both mammalian Spir proteins, Spir-1 and Spir-2, interact with mammalian Fmn subgroup proteins formin-1 and formin-2
FlnA and Fmn2 are likely essential to cell proliferation, differentiation and cell death in a variety of tissues and organs, further reiterating the importance of vesicle trafficking in regulation of development
Fmn2 as a mediator of actin bundle integrity, enabling efficient force transmission to the adhesion sites.
Data suggest formin homology domain (FH2) of Fmn2 binds actin at filament barbed end as weak capper and plays a role in displacing WASP homology domain 2 (WH2) domains of Spire-1 from actin; competitive binding of Fmn2 vs Spire-1 aids actin assembly.
Spire recruits Fmn2 and facilitates its association with actin filaments barbed ends.
Results suggest that the regulation of microtubule acetylation is likely a general formin activity.
Spire1 and Spire2 cooperate with Formin-2 (Fmn2) to nucleate actin filaments in mouse oocytes.
High formin 2 levels at meiosis I entry induce meshwork maintenance, leading to equal forces being exerted on the chromosomes, preventing spindle migration.
Gene profiling of Fmn2 in Graffi murine leukemia virus-induced lymphoid leukemias suggest its important role in leukemogenesis.
Fmn2 is a candidate in a QTL hotspot associated with neurobehavioral traits and gene expression in the mouse brain. Hippocampal pyramidal neurons exhibit distinct and fine granular immunoreactivity for FMN2.
formin-2 is a maternal-effect gene that is expressed in oocytes and is required for progression through metaphase of meiosis I
The mouse formin-2 gene has been found to be expressed in the developing nervous system and in neuronal cells of the adult brain.
It is likely that human FMN2 has the same function as Fmn2 in the mouse (i.e., maintenance of the meiotic spindle).
Formin homology (FH) domain proteins (see FMN1\; MIM 136535) play a role in cytoskeletal organization and/or establishment of cell polarity.
, formin 2
, LOW QUALITY PROTEIN: formin-2
, formin 2-like