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FBLIM1 encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. Additionally we are shipping FBLIM1 Antibodies (50) and FBLIM1 Kits (9) and many more products for this protein.
Showing 6 out of 7 products:
data implicate FBLIM1 in the pathogenesis of sterile bone inflammation and our findings suggest CRMO is a disorder of chronic inflammation and imbalanced bone remodeling
the present study emphasizes for the first time to our knowledge the role of Migfilin in osteoarthritis(OA) and highlights the importance of cell-ECM (show MMRN1 Proteins) adhesion proteins in OA pathogenesis.
Migfilin expression is reduced in breast cancer.
alpha-parvin (show PARVA Proteins), beta-parvin (show PARVB Proteins) and migfilin were expressed in tumor cells in 53%, 2%, 28% and 53% of effusions and 57%, 20%, 83% and 25% of solid lesions, respectively.
Migfilin positively modulates the expression and activity of epidermal growth factor receptor (show EGFR Proteins), and Migfilin-mediated migration and invasion depend on epidermal growth factor receptor (show EGFR Proteins)-induced PLC (show HSPG2 Proteins)-gamma and STAT3 (show STAT3 Proteins)-signaling pathways.
Migfilin promoted beta-catenin degradation by reinforcing the association between beta-catenin and GSK-3beta.
Migfilin can activate beta1, beta2 and beta3 integrins and promote integrin mediated responses while migfilin depletion impairs the spreading and migration of endothelial cells
The association between filamin B (show FLNB Proteins) and FBLP-1 may play a hitherto unknown role in cytoskeletal function, cell adhesion, and cell motility.
Migfilin has a role in interacting with vasodilator-stimulated phosphoprotein (VASP (show VASP Proteins)) and regulates VASP (show VASP Proteins) localization to cell-matrix adhesions and migration
Results suggest a role for cytoplasmic migfilin in the progression of leiomyosarcomas (LMS) and identify cytoplasmic migfilin as a potentially important biological marker for human LMS progression.
Suggest migfilin regulates cardiac hypertrophy in transverse aortic constriction.
C-terminal LIM (show PDLIM5 Proteins) domains of migfilin dictate its focal adhesion localization, and these domains mediate an interaction with kindlin in vitro and in cells, demonstrating that kindlin is important for normal migfilin dynamics.
results identify FBLP-1 as a key regulator of bone homeostasis and suggest that FBLP-1 functions in this process through modulating both the intrinsic properties of OB/BMSCs (i.e., BMSC-extracellular matrix adhesion and migration
This study demonistrated that a molecular mechanism whereby FlnA (show FLNA Proteins) loss impaired G2 to M phase entry, leading to cell cycle prolongation, compromised neural progenitor proliferation, and reduced brain size.
The findings indicate that the roles of migfilin are functionally redundant during mouse development and tissue homeostasis.
results suggest that a novel LIM protein (show PDLIM1 Proteins) Cal (show S100A11 Proteins) induces cardiomyocyte differentiation through its dynamic intracellular shuttling and association with CSX/NKX2-5 (show NKX2-5 Proteins)
analysis of the migfilin-filamin (show FLNA Proteins) interaction and competition with integrin beta 7 (show ITGB7 Proteins) tails
This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.
filamin binding LIM protein 1
, filamin-binding LIM protein-1
, filamin-binding LIM protein 1
, CSX-associated LIM
, MIG2-interacting protein
, mitogen-inducible 2 interacting protein
, mitogen-inducible 2-interacting protein