Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Cell motility is a basic cellular behavior involved in embryogenesis, neurite outgrowth, wound healing, inflammation, and cancer metastasis. Filamentous actin is an essential component of cell protrusions involved in cell motility. The protrusion formation is regulated by actin polymerization and depolymerization. Cofilin is a ubiquitously expressed G- and F-actin binding protein that contains a nuclear localization signal, a C-terminal hexapeptide sequence that is identical to tropomyosin, and other regions that are homologous to actin binding proteins. In vitro, cofilin has actin severing activity and induces an increased off-rate from the pointed end of actin filaments. These activities can increase the rate of actin polymerization and depolymerization, as well as increase the number of barbed ends available for polymerization. Stimulation of MTLn3 cells with EGF leads to an increase in cofilin at the leading edge of laemellipodia, which correlates with an increase in the number of barbed ends at the leading edge. Cofilin function blocking antibodies inhibit both the appearance of these barbed ends and lamellipodial protrusion. Thus, cofilin is an actin binding protein that regulates actin filament formation during cell motility.
Development References (3)
-
Chan AY, Bailly M, Zebda N, Segall JE, Condeelis JS. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J Cell Biol. 2000; 148(3):531-542. (Biology). View Reference
-
Moriyama K, Matsumoto S, Nishida E, Sakai H, Yahara I. Nucleotide sequence of mouse cofilin cDNA. Nucleic Acids Res. 1990; 18(10):3053. (Biology). View Reference
-
Moriyama K, Yahara I. Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are affected differentially by mutations around the actin-binding helix. EMBO J. 1999; 18(23):6752-6761. (Biology). View Reference
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.