Filamin is a large (270kd) dimeric actin crosslinking protein from a variety of sources, which helps to stabilize the 3D cortical actin network. The fundamental structure of filamin is well conserved and consists of an actin binding domain at the N-terminus followed by a C-terminal rod domain consisting of numerous repeat segments ranging from 4 in C. elegans to 24 in mammalian cells. Each repeat in the rod domain consists of roµghly 100 residues and forms an immunoglobulin like fold. Such immunoglobulin folds have been found in a variety of proteins and are responsible for protein-protein interactions. Filamin Human actin-binding protein (ABP), aka filamin, crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Mammalian filamin interacts directly with at least 30 proteins such as transmembrane receptors, second messenger-associated proteins, protein kinases, phosphatases and cytoskeletal proteins and these interactions have been shown to require one or more of the repeat elements in the rod domain.
Sterile Filtered White lyophilized (freeze-dried) powder.
The protein was lyophilized from a 1mg/ml solution containing 20mM Tris / acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT and 20mM NaCl. Each mg Filamin contains 550mg urea.
It is recommended to reconstitute the lyophilized Filamin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Lyophilized Filamin althoµgh stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Filamin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Greater than 90.0% as determined by SDS-PAGE.
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Protein standard in 1D and 2D SDS gelelectrophoresisImmunoassays Immunization.