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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. Zusätzlich bieten wir Ihnen FBLIM1 Kits (11) und FBLIM1 Proteine (7) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 49 products:
Human Monoclonal FBLIM1 Primary Antibody für ELISA, WB - ABIN565770
Has, Herz, Zimina, Qu, He, Zhang, Wen, Gache, Aumailley, Bruckner-Tuderman: Kindlin-1 Is required for RhoGTPase-mediated lamellipodia formation in keratinocytes. in The American journal of pathology 2009
Human Polyclonal FBLIM1 Primary Antibody für ICC, IF - ABIN4334514
Li, Ponten, dos Remedios: The interactome of LIM domain proteins: the contributions of LIM domain proteins to heart failure and heart development. in Proteomics 2012
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 (zeige MMRN1 Antikörper) adhesion proteins in OA pathogenesis.
Migfilin expression is reduced in breast cancer.
alpha-parvin (zeige PARVA Antikörper), beta-parvin (zeige PARVB Antikörper) 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 (zeige EGFR Antikörper), and Migfilin-mediated migration and invasion depend on epidermal growth factor receptor (zeige EGFR Antikörper)-induced PLC (zeige HSPG2 Antikörper)-gamma and STAT3 (zeige STAT3 Antikörper)-signaling pathways.
Migfilin promoted beta-catenin (zeige CTNNB1 Antikörper) degradation by reinforcing the association between beta-catenin (zeige CTNNB1 Antikörper) and GSK-3beta (zeige GSK3b Antikörper).
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 (zeige FLNB Antikörper) 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 (zeige VASP Antikörper)) and regulates VASP (zeige VASP Antikörper) 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 (zeige PDLIM5 Antikörper) 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 (zeige FLNA Antikörper) 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 (zeige PDLIM1 Antikörper) Cal (zeige S100A11 Antikörper) induces cardiomyocyte differentiation through its dynamic intracellular shuttling and association with CSX/NKX2-5 (zeige NKX2-5 Antikörper)
analysis of the migfilin-filamin (zeige FLNA Antikörper) interaction and competition with integrin beta 7 (zeige ITGB7 Antikörper) 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