FLNC Antibody

FLNC, Filamin-c, Filamin-2 (FLN2), Actin binding-like protein (APBL) (290.8 kDa) is an isoform of the Filamin proteins family. Filamins are broadly expressed and function as actin-binding and actin-crosslinking proteins. Structurally, Filamins consist of three main domains; N-terminal actin-binding domain, multiple central immunoglobulin (Ig) domains, and a C-terminal domain which supports homodimerization (1, 2). Functionally, Filamins play a role in cytoskeleton structure through interactions with actin, but they are implicated in a wide range of processes through their interactions with diverse molecular partners such as signaling molecules (MKK4, JNK1), ion channels (Kv4.2, Kir2.1), receptors (Insulin, Calcitonin), and transcription factors (Smad1-6, Foxc1) (3).

Three isoforms of Filamin are expressed in mammals, identified as FLNA, FLNB and FLNC. FLNC is considered a muscle specific Filamin isoform for its high expression in cardiac and skeletal muscles. In muscle tissue, FLNC localizes to the Z-line, sarcolemma, myotendinous and intercalated disks (2). FLNC interacts with various muscle proteins via a non-conserved sequence within its Ig domain 20. Some muscle binding partners for FLNC include gamma and delta-sarcoglycans in the sarcolemma, and FATZ, myozenins, myotilin and myopodin in the Z-discs (2, 4). FLNC variants are associated with various inherited pathological conditions including myofibrillar myopathy 5, distal myopathy 4, dilated cardiomyopathy, hypertrophic cardiomyopathy, and restrictive cardiomyopathy (2, 5).

References

1. Chiang, W., Greaser, M. L., & Lyons, G. E. (2000). Filamin isogene expression during mouse myogenesis. Developmental Dynamics. https://doi.org/10.1002/(sici)1097-0177(200001)217:1<99::aid-dvdy9>3.3.co;2-x

2. Leber, Y., Ruparelia, A. A., Kirfel, G., van der Ven, P. F. M., Hoffmann, B., Merkel, R., ... Furst, D. O. (2016). Filamin C is a highly dynamic protein associated with fast repair of myofibrillar microdamage. Human Molecular Genetics. https://doi.org/10.1093/hmg/ddw135

3. Nakamura, F., Stossel, T. P., & Hartwig, J. H. (2011). The filamins: Organizers of cell structure and function. Cell Adhesion and Migration. https://doi.org/10.4161/cam.5.2.14401

4. Thompson, T. G., Chan, Y. M., Hack, A. A., Brosius, M., Rajala, M., Lidov, H. G. W., ... Kunkel, L. M. (2000). Filamin 2 (FLN2): A muscle-specific sarcoglycan interacting protein. Journal of Cell Biology. https://doi.org/10.1083/jcb.148.1.115

5. Brodehl, A., Ferrier, R. A., Hamilton, S. J., Greenway, S. C., Brundler, M. A., Yu, W., ... Scherer, S. (2016). Mutations in FLNC are Associated with Familial Restrictive Cardiomyopathy. Human Mutation. https://doi.org/10.1002/humu.22942

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 3 applications: IHC-P, WB, Western Blot.

Showing Publications 1 - 9 of 9.

Publications using NBP1-89300	Applications	Species
Marion Onnée, Audrey Bénézit, Sultan Bastu, Aleksandra Nadaj-Pakleza, Béatrice Lannes, Flavie Ader, Corinne Thèze, Pascal Cintas, Claude Cances, Robert-Yves Carlier, Corinne Metay, Mireille Cossée, Edoardo Malfatti, Paul Rösch The FLNC Ala1186Val Variant Linked to Cytoplasmic Body Myopathy and Cardiomyopathy Causes Protein Instability Biomedicines 2024-01-30 [PMID: 38397924]
Yerra VG, Batchu SN, Kaur H et al. Pressure overload induces ISG15 to facilitate adverse ventricular remodeling and promote heart failure The Journal of clinical investigation 2023-05-01 [PMID: 37115698] (WB, IHC-P, Mouse)	WB, IHC-P	Mouse
Wu T, Xu Y, Zhang L et al. Filamin C is Essential for mammalian myocardial integrity PLOS Genetics 2023-01-27 [PMID: 36706168] (Western Blot)	Western Blot
Knyazeva A, Khudiakov A, Vaz R et al. FLNC Expression Level Influences the Activity of TEAD-YAP/TAZ Signaling Nat Commun 2020-11-13 [PMID: 33202721] (WB, Human, Mouse)	WB	Human, Mouse
Robertson R, Conte TC, Dicaire MJ et al. BAG3P215L/KO Mice as a Model of BAG3P209L Myofibrillar Myopathy Am. J. Pathol. 2020-01-14 [PMID: 31953038]
Kiselev A, Vaz R, Knyazeva A et al. De novo mutations in FLNC leading to early-onset restrictive cardiomyopathy and congenital myopathy Hum. Mutat. 2018-06-01 [PMID: 29858533] (Human)		Human
Wu T, Mu Y, Bogomolovas J et al. HSPB7 is indispensable for heart development by modulating actin filament assembly. Proc. Natl. Acad. Sci. U.S.A. 2017-10-23 [PMID: 29078393] (Mouse)		Mouse
Reinstein E, Gutierrez-Fernandez A, Tzur S et al. Congenital dilated cardiomyopathy caused by biallelic mutations in Filamin C. Eur. J. Hum. Genet. 2016-09-07 [PMID: 27601210] (IHC-P)	IHC-P
Valdes-Mas R, Gutierrez-Fernandez A, Gomez J et al. Mutations in filamin C cause a new form of familial hypertrophic cardiomyopathy Nat Commun et al. 2014-10-29 [PMID: 25351925] (IHC-P, Human) Details: FLnC/Filamin C antibody used for IHC-P on heart tissue sectionsfrom human control subjects and three hypertrophic cardiomyopathy patien - tone caused by a mutation in MYH7, and two without mutations in sarcomeric genes or FLnC, revealed large nuclei and larger fibre diameter, but not filamin C aggregates. IHC revealed the presence of FLnC in the protein aggregate occurring in cardiomyocytes of patients with FLnC mutations (Figure 3c).	IHC-P	Human

Images	Ratings	Applications	Species	Date	Details
	4 reviewed by: Pankaj Pathak	IHC-Fr	Mouse	06/28/2021	View Summary Application Immunohistochemistry-Frozen Sample Tested Mouse skeletal muscle,Skeletal muscle tissue Species Mouse Lot 0113767 Comments Comments Pathak, P., Blech-Hermoni, Y., Subedi, K. et al. Myopathy associated LDB3 mutation causes Z-disc disassembly and protein aggregation through PKC alpha and TSC2-mTOR downregulation. Commun Biol 4, 355 (2021). https://doi.org/10.1038/s42003-021-01864-1 ***Novus Innovators Program - new species or application used on a primary antibody.

Array NBP1-89300

• FLNC Antibodies
• FLNC ELISA Kits
• FLNC Proteins