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WH0054751M10

Sigma-Aldrich

Monoclonal Anti-FBLIM1 antibody produced in mouse

clone 5E11, purified immunoglobulin, buffered aqueous solution

Sinonimo/i:

Anti-CAL, Anti-DKFZp434G171, Anti-FBLP1, Anti-RP11169K16.5, Anti-filamin binding LIM protein 1

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

5E11, monoclonal

Forma fisica

buffered aqueous solution

Reattività contro le specie

human

tecniche

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

Isotipo

IgG2aκ

N° accesso Genebanck

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... FBLIM1(54751)

Descrizione generale

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)

Immunogeno

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

Azioni biochim/fisiol

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.

Stato fisico

Solution in phosphate buffered saline, pH 7.4

Note legali

GenBank is a registered trademark of United States Department of Health and Human Services

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificati d'analisi (COA)

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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)
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)
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 regulates esophageal cancer cell motility through promoting GSK-3?-mediated degradation of ?-catenin.
He H, et al.
Molecular Cancer Research, 10, 273-281 (2012)

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