Monoclonal Anti-FBLIM1, (C-terminal) antibody produced in mouse

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. (provided by RefSeq)

FBLIM1 (NP_060026, 270 a.a. ~ 373 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
VTCARCIGDESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC

FBLIM1 (filamin binding LIM protein 1) plays an important role in association between the cell membrane and the actin cytoskeleton. It mainly interacts with MIG-2 (mitogen-inducible gene 2 protein), filamin and VASP (vasodilator-stimulated phosphoprotein), thus controlling cell shape and movements. In cardiomyocytes, it interacts with transcription factor CSX/NKX2-5 (cardiac-specific homeobox) and enhances the differentiation. The FBLIM1 gene is upregulated in osteoarthritis chondrocytes and might be involved with osteoarthritis pathogenesis. In various carcinoma cells, the FBLIM1-associated signaling in disrupted which leads to abnormal Src activation and anoikis resistance in cells. This gene is downregulated in breast cancer cells. In esophageal cancer cells, it suppresses invasion partly by enhancing degradation of β-catenin. However, in glioma cells FBLIM1 promotes migration as well as invasion.

Solution in phosphate buffered saline, pH 7.4