Key features and details
- Rabbit polyclonal to Filamin A
- Suitable for: WB
- Reacts with: Human
- Isotype: IgG
- Research with confidence – consistent and reproducible results with every batch
- Long-term and scalable supply – powered by recombinant technology for fast production
- Success from the first experiment – confirmed specificity through extensive validation
- Ethical standards compliant – production is animal-free
Product nameAnti-Filamin A antibody
See all Filamin A primary antibodies
DescriptionRabbit polyclonal to Filamin A
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Human
A synthesized non-phosphopeptide derived from human Filamin A around the phosphorylation site of serine 2152 (A-P-SP-V-A).
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Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, PBS
Concentration information loading...
PurityImmunogen affinity purified
Purification notesThe antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
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Our Abpromise guarantee covers the use of ab51217 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/300 - 1/1000. Detects a band of approximately 281 kDa (predicted molecular weight: 281 kDa).
1/300 - 1/1000. Detects a band of approximately 281 kDa (predicted molecular weight: 281 kDa).
FunctionPromotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking.
Involvement in diseaseDefects in FLNA are the cause of periventricular nodular heterotopia type 1 (PVNH1) [MIM:300049]; also called nodular heterotopia, bilateral periventricular (NHBP or BPNH). PVNH is a developmental disorder characterized by the presence of periventricular nodules of cerebral gray matter, resulting from a failure of neurons to migrate normally from the lateral ventricular proliferative zone, where they are formed, to the cerebral cortex. PVNH1 is an X-linked dominant form. Heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. Hemizygous affected males die in the prenatal or perinatal period.
Defects in FLNA are the cause of periventricular nodular heterotopia type 4 (PVNH4) [MIM:300537]; also known as periventricular heterotopia Ehlers-Danlos variant. PVNH4 is characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilation in early adulthood.
Defects in FLNA are the cause of otopalatodigital syndrome type 1 (OPD1) [MIM:311300]. OPD1 is an X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato-digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum.
Defects in FLNA are the cause of otopalatodigital syndrome type 2 (OPD2) [MIM:304120]; also known as cranioorodigital syndrome. OPD2 is a congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects.
Defects in FLNA are the cause of frontometaphyseal dysplasia (FMD) [MIM:305620]. FMD is a congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies.
Defects in FLNA are the cause of Melnick-Needles syndrome (MNS) [MIM:309350]. MNS is a severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull.
Defects in FLNA are the cause of X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX) [MIM:300048]. CIIPX is characterized by a severe abnormality of gastrointestinal motility due to primary qualitative defects of enteric ganglia and nerve fibers. Affected individuals manifest recurrent signs of intestinal obstruction in the absence of any mechanical lesion.
Defects in FLNA are the cause of FG syndrome type 2 (FGS2) [MIM:300321]. FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.
Defects in FLNA are the cause of terminal osseous dysplasia (TOD) [MIM:300244]. A rare X-linked dominant male-lethal disease characterized by skeletal dysplasia of the limbs, pigmentary defects of the skin and recurrent digital fibroma during infancy. A significant phenotypic variability is observed in affected females.
Defects in FLNA are the cause of cardiac valvular dysplasia X-linked (CVDX) [MIM:314400]. A rare X-linked heart disease characterized by mitral and/or aortic valve regurgitation. The histologic features include fragmentation of collagenous bundles within the valve fibrosa and accumulation of proteoglycans, which produces excessive valve tissue leading to billowing of the valve leaflets.
Sequence similaritiesBelongs to the filamin family.
Contains 1 actin-binding domain.
Contains 2 CH (calponin-homology) domains.
Contains 24 filamin repeats.
DomainComprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation.
modificationsPhosphorylated upon DNA damage, probably by ATM or ATR (By similarity). Phosphorylation extent changes in response to cell activation.
The N-terminus is blocked.
Cellular localizationCytoplasm > cell cortex. Cytoplasm > cytoskeleton.
- Information by UniProt
- ABP 280 antibody
- ABP-280 antibody
- Actin-binding protein 280 antibody
ab51217 has been referenced in 10 publications.
- Speight P et al. Context-dependent switch in chemo/mechanotransduction via multilevel crosstalk among cytoskeleton-regulated MRTF and TAZ and TGFß-regulated Smad3. Nat Commun 7:11642 (2016). PubMed: 27189435
- Zhang L et al. Tsc1 haploinsufficiency is sufficient to increase dendritic patterning and Filamin A levels. Neurosci Lett 629:15-18 (2016). PubMed: 27345385
- Holle AW et al. High content image analysis of focal adhesion-dependent mechanosensitive stem cell differentiation. Integr Biol (Camb) 8:1049-1058 (2016). PubMed: 27723854
- Hofmeister LH et al. Phage-display-guided nanocarrier targeting to atheroprone vasculature. ACS Nano 9:4435-46 (2015). PubMed: 25768046
- Mizuhashi K et al. Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the formation of cartilaginous skeletal elements. Hum Mol Genet N/A:N/A (2014). Mouse . PubMed: 24436304
- Adams M et al. A meckelin-filamin A interaction mediates ciliogenesis. Hum Mol Genet 21:1272-86 (2012). ICC/IF ; Human . PubMed: 22121117
- Mooso BA et al. Enhancing the effectiveness of androgen deprivation in prostate cancer by inducing Filamin A nuclear localization. Endocr Relat Cancer 19:759-77 (2012). ICC/IF ; Human . PubMed: 22993077
- Gawecka JE et al. RSK2 Protein Suppresses Integrin Activation and Fibronectin Matrix Assembly and Promotes Cell Migration. J Biol Chem 287:43424-37 (2012). WB . PubMed: 23118220
- Sayner SL et al. Filamin A is a phosphorylation target of membrane but not cytosolic adenylyl cyclase activity. Am J Physiol Lung Cell Mol Physiol 301:L117-24 (2011). WB, ICC/IF ; Rat . PubMed: 21478251
- Cooper J et al. Filamin a protein interacts with human immunodeficiency virus type 1 gag protein and contributes to productive particle assembly. J Biol Chem 286:28498-510 (2011). Flow Cyt ; Human . PubMed: 21705339