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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. 再加上，我们可以发FBLIM1 抗体 (50) 和 FBLIM1 蛋白 (7)和数多这个蛋白质的别的产品。
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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 (显示 MMRN1 ELISA试剂盒) adhesion proteins in OA pathogenesis.
Migfilin expression is reduced in breast cancer.
alpha-parvin (显示 PARVA ELISA试剂盒), beta-parvin (显示 PARVB ELISA试剂盒) 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 (显示 EGFR ELISA试剂盒), and Migfilin-mediated migration and invasion depend on epidermal growth factor receptor (显示 EGFR ELISA试剂盒)-induced PLC (显示 HSPG2 ELISA试剂盒)-gamma and STAT3 (显示 STAT3 ELISA试剂盒)-signaling pathways.
Migfilin promoted beta-catenin (显示 CTNNB1 ELISA试剂盒) degradation by reinforcing the association between beta-catenin (显示 CTNNB1 ELISA试剂盒) and GSK-3beta (显示 GSK3b ELISA试剂盒).
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 (显示 FLNB ELISA试剂盒) 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 (显示 VASP ELISA试剂盒)) and regulates VASP (显示 VASP ELISA试剂盒) 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 (显示 PDLIM5 ELISA试剂盒) 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 (显示 FLNA ELISA试剂盒) 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 (显示 PDLIM1 ELISA试剂盒) Cal (显示 S100A11 ELISA试剂盒) induces cardiomyocyte differentiation through its dynamic intracellular shuttling and association with CSX/NKX2-5 (显示 NKX2-5 ELISA试剂盒)
analysis of the migfilin-filamin (显示 FLNA ELISA试剂盒) interaction and competition with integrin beta 7 (显示 ITGB7 ELISA试剂盒) 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