Product: Filamin A Mouse Monoclonal Antibody
Catalog: BF8885
Description: Mouse monoclonal antibody to Filamin A
Application: WB
Reactivity: Human
Prediction: Mouse, Rat, Pig, Bovine, Horse, Sheep, Rabbit, Dog
Mol.Wt.: 280kDa; 281kD(Calculated).
Uniprot: P21333

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Product Info

Source:
Mouse
Application:
WB 1:500-1:3000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human
Clonality:
Monoclonal [AFfirm8885]
Specificity:
Filamin A Mouse Monoclonal Antibody detects endogenous levels of total Filamin A.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

ABP 280; ABP-280; Actin-binding protein 280; Alpha filamin; Alpha-filamin; APBX; CSBS; CVD1; Endothelial actin binding protein; Endothelial actin-binding protein; Filamin 1; Filamin A alpha; Filamin A; Filamin-1; Filamin-A; FLN; FLN-A; FLN1; FLNA; FLNA_HUMAN; FMD; MNS; NHBP; Non muscle filamin; Non-muscle filamin; OPD; OPD1; OPD2; XLVD; XMVD;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P21333 FLNA_HUMAN:

Ubiquitous.

Sequence:
MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP

PTMs - P21333 As Substrate

Site PTM Type Enzyme
S2 Acetylation
S2 Phosphorylation
S3 Phosphorylation
S4 Phosphorylation
S6 Phosphorylation
R7 Methylation
S11 Phosphorylation
T23 Phosphorylation
T31 Phosphorylation
K33 Ubiquitination
K42 Acetylation
K42 Methylation
K42 Ubiquitination
K43 Ubiquitination
T48 Phosphorylation
T50 Phosphorylation
K58 Ubiquitination
T69 Phosphorylation
S72 Phosphorylation
S85 Phosphorylation
K87 Ubiquitination
K88 Ubiquitination
K92 Ubiquitination
K120 Ubiquitination
S123 Phosphorylation
K135 Ubiquitination
K169 Acetylation
T186 Phosphorylation
S189 Phosphorylation
S204 Phosphorylation
S215 Phosphorylation
K220 Ubiquitination
K270 Ubiquitination
Y287 Phosphorylation
K299 Acetylation
K299 Sumoylation
K299 Ubiquitination
S310 Phosphorylation
Y319 Phosphorylation
T333 Phosphorylation
K367 Ubiquitination
S368 Phosphorylation
Y373 Phosphorylation
K376 Acetylation
K376 Ubiquitination
S377 Phosphorylation
S382 Phosphorylation
K383 Ubiquitination
T385 Phosphorylation
S394 Phosphorylation
Y403 Phosphorylation
S440 Phosphorylation
C444 S-Nitrosylation
S468 Phosphorylation
Y470 Phosphorylation
T471 Phosphorylation
C478 S-Nitrosylation
S481 Phosphorylation
C483 S-Nitrosylation
T500 Phosphorylation
K504 Acetylation
K504 Ubiquitination
Y506 Phosphorylation
T507 Phosphorylation
K508 Acetylation
K508 Ubiquitination
S512 Phosphorylation
T518 Phosphorylation
Y538 Phosphorylation
K578 Acetylation
K578 Ubiquitination
R580 Methylation
C623 S-Nitrosylation
K626 Acetylation
S630 Phosphorylation
C631 S-Nitrosylation
Y643 Phosphorylation
S651 Phosphorylation
S657 Phosphorylation
R674 Methylation
K684 Ubiquitination
T685 Phosphorylation
K691 Methylation
K691 Ubiquitination
K700 Acetylation
K700 Ubiquitination
K704 Ubiquitination
C717 S-Nitrosylation
T730 Phosphorylation
Y731 Phosphorylation
S732 Phosphorylation
C733 S-Nitrosylation
S734 Phosphorylation
Y735 Phosphorylation
S748 Phosphorylation
S753 Phosphorylation
S757 Phosphorylation
S767 Phosphorylation
K771 Acetylation
K771 Ubiquitination
K773 Ubiquitination
Y775 Phosphorylation
K781 Acetylation
K781 Ubiquitination
T782 Phosphorylation
T790 Phosphorylation
Y791 Phosphorylation
T793 Phosphorylation
C810 S-Nitrosylation
K837 Acetylation
K837 Ubiquitination
T859 Phosphorylation
S860 Phosphorylation
K865 Acetylation
K865 Ubiquitination
S869 Phosphorylation
K874 Acetylation
K876 Ubiquitination
S883 Phosphorylation
K891 Acetylation
K891 Ubiquitination
K906 Acetylation
K906 Ubiquitination
S912 Phosphorylation
T915 Phosphorylation
K916 Ubiquitination
Y933 Phosphorylation
T950 Phosphorylation
K958 Ubiquitination
S959 Phosphorylation
S962 Phosphorylation
S966 Phosphorylation
S968 Phosphorylation
S972 Phosphorylation
K973 Acetylation
K973 Ubiquitination
K975 Ubiquitination
S977 Phosphorylation
K982 Ubiquitination
K987 Acetylation
K987 Ubiquitination
K994 Acetylation
K1003 Ubiquitination
K1007 Ubiquitination
C1018 S-Nitrosylation
K1019 Acetylation
K1019 Ubiquitination
S1029 Phosphorylation
Y1047 Phosphorylation
S1055 Phosphorylation
K1071 Acetylation
K1071 Ubiquitination
S1081 Phosphorylation
S1084 Phosphorylation P06493 (CDK1)
R1087 Methylation
T1089 Phosphorylation
C1157 S-Nitrosylation
S1161 Phosphorylation
K1162 Acetylation
K1162 Ubiquitination
K1164 Ubiquitination
K1246 Ubiquitination
T1255 Phosphorylation
C1260 S-Nitrosylation
Y1261 Phosphorylation
S1279 Phosphorylation
T1286 Phosphorylation
T1288 Phosphorylation
K1294 Ubiquitination
S1301 Phosphorylation
T1305 Phosphorylation
T1307 Phosphorylation
Y1308 Phosphorylation
R1312 Methylation
T1334 Phosphorylation
S1338 Phosphorylation
S1343 Phosphorylation
S1367 Phosphorylation
K1372 Ubiquitination
K1375 Acetylation
T1377 Phosphorylation
T1385 Phosphorylation
S1396 Phosphorylation
K1399 Ubiquitination
S1436 Phosphorylation P06493 (CDK1)
T1446 Phosphorylation
S1449 Phosphorylation
K1452 Ubiquitination
C1453 S-Nitrosylation
S1454 Phosphorylation
S1459 Phosphorylation P06493 (CDK1)
S1470 Phosphorylation
T1475 Phosphorylation
S1476 Phosphorylation
K1477 Ubiquitination
K1486 Ubiquitination
K1491 Ubiquitination
T1506 Phosphorylation
Y1511 Phosphorylation
S1514 Phosphorylation
S1520 Phosphorylation
S1522 Phosphorylation
Y1525 Phosphorylation
S1533 Phosphorylation P06493 (CDK1)
K1538 Acetylation
K1538 Ubiquitination
K1547 Ubiquitination
S1551 Phosphorylation
T1557 Phosphorylation
S1563 Phosphorylation
T1585 Phosphorylation
K1590 Ubiquitination
T1594 Phosphorylation
T1603 Phosphorylation
Y1604 Phosphorylation
T1605 Phosphorylation
T1617 Phosphorylation
K1621 Ubiquitination
Y1622 Phosphorylation
S1630 Phosphorylation P06493 (CDK1)
Y1632 Phosphorylation
T1639 Phosphorylation
Y1720 Phosphorylation
S1734 Phosphorylation
T1739 Phosphorylation
Y1761 Phosphorylation
T1762 Phosphorylation
Y1763 Phosphorylation
K1801 Ubiquitination
K1814 Ubiquitination
K1824 Acetylation
K1824 Ubiquitination
S1835 Phosphorylation
S1854 Phosphorylation
Y1862 Phosphorylation
Y1871 Phosphorylation
S1899 Phosphorylation
S1906 Phosphorylation
C1912 S-Nitrosylation
C1920 S-Nitrosylation
Y1932 Phosphorylation
K1937 Ubiquitination
Y1938 Phosphorylation
S1946 Phosphorylation
S1961 Phosphorylation
K1964 Ubiquitination
S1967 Phosphorylation
S1976 Phosphorylation
S1981 Phosphorylation
T1984 Phosphorylation
S1991 Phosphorylation
K2000 Acetylation
K2000 Ubiquitination
S2010 Phosphorylation
K2024 Ubiquitination
S2033 Phosphorylation
S2053 Phosphorylation
T2062 Phosphorylation
S2088 Phosphorylation
S2128 Phosphorylation
S2131 Phosphorylation
K2133 Ubiquitination
T2135 Phosphorylation
K2141 Ubiquitination
S2143 Phosphorylation
T2145 Phosphorylation
S2152 Phosphorylation P31749 (AKT1) , Q15418 (RPS6KA1) , P17612 (PRKACA) , Q13153 (PAK1)
S2158 Phosphorylation
S2163 Phosphorylation
S2180 Phosphorylation
S2182 Phosphorylation
K2184 Ubiquitination
Y2198 Phosphorylation
C2199 S-Nitrosylation
T2209 Phosphorylation
S2213 Phosphorylation
K2217 Methylation
K2217 Ubiquitination
S2224 Phosphorylation
T2229 Phosphorylation
K2240 Ubiquitination
R2242 Methylation
S2260 Phosphorylation
S2284 Phosphorylation
K2289 Ubiquitination
S2292 Phosphorylation Q13153 (PAK1)
C2293 S-Nitrosylation
Y2305 Phosphorylation
S2308 Phosphorylation
S2319 Phosphorylation
S2327 Phosphorylation
T2336 Phosphorylation
S2338 Phosphorylation
S2339 Phosphorylation
S2343 Phosphorylation
S2352 Phosphorylation
S2356 Phosphorylation
K2361 Ubiquitination
K2367 Ubiquitination
S2370 Phosphorylation Q13153 (PAK1)
S2372 Phosphorylation
Y2379 Phosphorylation
T2381 Phosphorylation
K2387 Acetylation
K2387 Ubiquitination
Y2388 Phosphorylation
Y2400 Phosphorylation
S2414 Phosphorylation
K2417 Acetylation
K2417 Ubiquitination
K2473 Ubiquitination
C2476 S-Nitrosylation
C2479 S-Nitrosylation
Y2483 Phosphorylation
T2486 Phosphorylation
T2488 Phosphorylation
S2494 Phosphorylation
Y2505 Phosphorylation
S2510 Phosphorylation
K2513 Ubiquitination
S2523 Phosphorylation Q9UQM7 (CAMK2A)
S2526 Phosphorylation
S2537 Phosphorylation
K2540 Ubiquitination
T2542 Phosphorylation
C2543 S-Nitrosylation
K2563 Ubiquitination
K2569 Acetylation
K2569 Ubiquitination
Y2571 Phosphorylation
K2575 Ubiquitination
S2576 Phosphorylation
S2577 Phosphorylation
C2582 S-Nitrosylation
K2584 Ubiquitination
T2599 Phosphorylation
C2601 S-Nitrosylation
K2607 Acetylation
Y2614 Phosphorylation
S2615 Phosphorylation
S2617 Phosphorylation
K2621 Acetylation
K2623 Acetylation
K2623 Ubiquitination
Y2626 Phosphorylation
T2627 Phosphorylation
K2631 Ubiquitination
S2640 Phosphorylation
Y2642 Phosphorylation

Research Backgrounds

Function:

Promotes 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 FLNB 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 (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons.

PTMs:

Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA.

Phosphorylation extent changes in response to cell activation.

Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines. Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome.

Subcellular Location:

Cytoplasm>Cell cortex. Cytoplasm>Cytoskeleton. Perikaryon. Cell projection>Growth cone.
Note: Colocalizes with CPMR1 in the central region of DRG neuron growth cone (By similarity). Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By similarity).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Ubiquitous.

Subunit Structure:

Homodimer. Interacts with PDLIM2 (By similarity). Interacts with RFLNA and RFLNB (By similarity). Interacts with FCGR1A, FLNB, FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with MIS18BP1 (via N-terminus). Interacts (via N-terminus) with TAF1B. Interacts with TMEM67 (via C-terminus) and MKS1. Interacts (via actin-binding domain) with MICALL2 (via CH domain). Interacts (via filamin repeat 5) with SYK; docks SYK to the plasma membrane. Interacts (via filamin repeats 19 and 21) with DRD3; increased PKA-mediated phosphorylation at Ser-2152. Interacts (via filamin repeat 21) with MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA at Ser-2152. Interacts (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1. Interacts with CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell scattering by interfering with the interaction between FLNA and RALA. Interacts with FOXC1. Interacts (via calponin-homology (CH) domain 1 and filamin repeat 24) with CRMP1; the interaction alters FLNA ternary structure and thus promotes FLNA dissociation from F-actin. Interacts with DPYSL3/CRMP3 and DPYSL4/CRMP4.

Family&Domains:

Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Filamin repeat 20 interacts with filamin repeat 21 masking the ligand binding site on filamin repeat 21, resulting in an autoinhibited conformation (PubMed:17690686). The autoinhibition can be relieved by ligands like ITGB7 or FBLIM1 (PubMed:21524097). Filamin repeats 19 and 21 can simultaneously engage ligands (PubMed:21524097).

Belongs to the filamin family.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Environmental Information Processing > Signal transduction > MAPK signaling pathway.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

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