SAB1409464
Anti-FBLIM1 antibody produced in mouse
purified immunoglobulin, buffered aqueous solution
Synonym(s):
CAL, DKFZp434G171, FBLP-1, FBLP1, RP11-169K16.5
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
6
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 41.03 kDa
species reactivity
human
technique(s)
western blot: 1 μg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... FBLIM1(54751)
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 (ABM85833.1, 1 a.a. ~ 373 a.a) full-length human protein.
Sequence
MASKPEKRVASSVFITLAPPRRDVAVAEEVRQAVCEARRGRPWEAPAPMKTPEAGLAGRPSPWTTPGRAAATVPAAPMQLFNGGCPPPPPVLDGEDVLPDLDLLPPPPPPPPVLLPSEEEAPAPMGASLIADLEQLHLSPPPPPPQAPAEGPSVQPGPLRPMEEELPPPPAEPVEKGASTDICAFCHKTVFPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKDGRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIGDESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC
Sequence
MASKPEKRVASSVFITLAPPRRDVAVAEEVRQAVCEARRGRPWEAPAPMKTPEAGLAGRPSPWTTPGRAAATVPAAPMQLFNGGCPPPPPVLDGEDVLPDLDLLPPPPPPPPVLLPSEEEAPAPMGASLIADLEQLHLSPPPPPPQAPAEGPSVQPGPLRPMEEELPPPPAEPVEKGASTDICAFCHKTVFPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKDGRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIGDESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC
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
Not finding the right product?
Try our Product Selector Tool.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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 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 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)
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)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service