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SAB1405134

Sigma-Aldrich

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

clone 3F8, purified immunoglobulin, buffered aqueous solution

Synonym(s):

CAL, DKFZp434G171, FBLP-1, FBLP1, RP11-169K16.5

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3F8, monoclonal

form

buffered aqueous solution

mol wt

antigen ~37.55 kDa

species reactivity

human

technique(s)

indirect ELISA: suitable
western blot: 1-5 μg/mL

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... FBLIM1(54751)

Related Categories

General description

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)

Immunogen

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

Biochem/physiol Actions

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.

Physical form

Solution in phosphate buffered saline, pH 7.4

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Migfilin, a-parvin and ?-parvin are differentially expressed in ovarian serous carcinoma effusions, primary tumors and solid metastases.
Davidson B, et al.
Gynecologic Oncology, 128, 364-370 (2013)
Migfilin protein promotes migration and invasion in human glioma through epidermal growth factor receptor-mediated phospholipase C-? and STAT3 protein signaling pathways.
Ou Y, et al.
The Journal of Biological Chemistry, 287, 32394-32405 (2012)
Mitogen-inducible Gene-2 (MIG2) and migfilin expression is reduced in samples of human breast cancer.
Gkretsi V, et al.
Anticancer Research, 33, 1977-1981 (2013)
Migfilin interacts with Src and contributes to cell-matrix adhesion-mediated survival signaling.
Zhao J, et al.
The Journal of Biological Chemistry, 284, 34308-34320 (2009)
Migfilin's elimination from osteoarthritic chondrocytes further promotes the osteoarthritic phenotype via ?-catenin upregulation.
Gkretsi V, et al.
Biochemical and Biophysical Research Communications, 430, 494-499 (2013)

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