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The protein encoded by BANF1 was first identified by its ability to protect retroviruses from intramolecular integration and therefore promote intermolecular integration into the host cell genome. Additionally we are shipping BANF1 Antibodies (76) and BANF1 Proteins (10) and many more products for this protein.
BAF plays essential roles in nuclear organization and that these BAF functions are required in both M phase and interphase of the cell cycle
BAF disappears at an early stage due to caspase (show CASP3 ELISA Kits) activity when apoptosis is induced by hid, and its depletion in mutants is sufficient in itself to induce cell death, suggesting it is an apoptotic mediator
BAF phosphorylation by NHK-1 disrupts anchorage of chromosomes to the nuclear envelope, allowing karyosome formation in oocytes.
Findings support the value of using BioID to identify unrecognized constituents of distinct subcellular compartments refractory to biochemical isolation and reveal VRK2A as a transmembrane kinase in the NE that regulates BAF.
It has been concluded that the LEM domain, responsible for binding to the chromatin protein BAF, undergoes a conformational change during self-assembly of emerin (show EMD ELISA Kits) N-terminal region.
antiviral capabilities of the barrier to autointegration factor (BAF/BANF1) and how its function and regulation places BAF at the junction of multiple pathways protecting a cell's genetic integrity
The findings unveil a unique mechanism where the nuclear periphery proteins lamin-A/C (show LMNA ELISA Kits), LAP2alpha and BAF1 are assembled into a protein complex during mitosis in order to regulate assembly and positioning of the mitotic spindle.
results demonstrate a novel function of BAF as an epigenetic regulator of HSV lytic infection; hypothesize that BAF facilitates Herpes Simplex Virus IE and E gene expression by recruiting the SETD1A (show SETD1A ELISA Kits) methyltransferase to viral IE and E gene promoters
Vaccinia virus B1 kinase is needed for multiple critical junctures in the poxviral life cycle in a manner that is both dependent on and independent of BAF.
BAF is a cytosolic DNA sensor that leads to exogenous DNA avoiding autophagy.
These data suggest that VRK3-mediated phosphorylation of BAF may facilitate DNA replication or gene expression by facilitating the dissociation of nuclear envelope proteins and chromatin during interphase.
Association of emerin (show EMD ELISA Kits) with nuclear BAF in cells required the LEM domain (residues 1-47).
The BANF1, alanine 12 threonine (A12T) mutant is impaired in its ability to bind DNA while its interaction with nuclear envelope proteins is unperturbed.
BAF can act in a phosphorylation-regulated (show PHAX ELISA Kits) manner to impair HSV-1 transcription and/or DNA replication.
Data determined that the knockdown of Banf1 alters the cell cycle distribution of both human and mouse ESCs (show NR2E3 ELISA Kits) by causing an uncharacteristic increase in the proportion of cells in the G2-M phase of the cell cycle.
HB and barrier-to-autointegration factor are the same protein
testicular cells display a 'Side Population' that express Bcrp1 mRNA, the ABC transporter (show TAP2 ELISA Kits) responsible for Hoechst efflux in hematopoietic cells
LAP2alpha stabilizes the association of BAF with the PIC to stimulate intermolecular integration and suppress autointegration.
Results suggest that Bcrp1 and P-gp (show ABCB4 ELISA Kits) transport topotecan into vCSF and out of brain parenchyma through the blood-brain barrier, and findings may help to improve pharmacologic strategies to treat brain tumors.
The protein encoded by this gene was first identified by its ability to protect retroviruses from intramolecular integration and therefore promote intermolecular integration into the host cell genome. The protein forms a homodimer which localizes to both the nucleus and cytoplasm and is specifically associated with chromosomes during mitosis. This protein binds to double stranded DNA in a non-specific manner and also binds to LEM-domain containing proteins of the nuclear envelope. This protein is thought to facilitate nuclear reassembly by binding with both DNA and inner nuclear membrane proteins and thereby recruit chromatin to the nuclear periphery. Alternative splicing results in multiple transcript variants encoding the same protein.
, barrier to autointegration factor 1
, barrier-to-autointegration factor
, breakpoint cluster region protein 1
, LAP2 binding protein 1
, LAP2-binding protein 1
, Breakpoint cluster region protein, uterine leiomyoma, 1
, Breakpoint cluster region protein, uterine leiomyoma, 1; barrier to autointegration factor
, Lap2 binding protein 1