• Biochemical analysis of cofilin1 functions
• Study the regulation of actin dynamics
• Positive control for actin binding/severing assays

Cofilin 1 is an actin-binding protein that regulates cytoskeletal dynamics by severing and depolymerizing actin filaments, playing a key role in cell motility, endocytosis, and signal transduction. It is essential for processes such as cell migration, neural development, and immune responses, and its dysregulation has been linked to cancer metastasis and neurodegenerative diseases.

The human cofilin protein (isotype 1) has been produced in a bacterial expression system.

• Purification tag: this protein does not have a recombinant tag
• Molecular weight: ~21 kDa
• Composition: when resuspended to 5 mg/ml, the buffer composition is 10 mM Tris pH 8.0, 10 mM NaCl, 5% sucrose, and 1% dextran.
• Supplied as a white lyophilized powder

Protein purity is determined by scanning densitometry of Coomassie Blue-stained protein on a 4-20% polyacrylamide gel. Purity is ≥95%

The biological activity of recombinant cofilin is assessed by its pH-dependent binding and severing of F-actin.

• pH 6.8: Cofilin binds F-actin at a 1:1 molar ratio (cofilin: actin) without severing. In spin-down assays, only ~20% of cofilin and actin appear in the supernatant; the pellet contains the 1:1 complex.
• pH 8.0: Cofilin severs F-actin, releasing ~80% of cofilin and actin into the supernatant.

Quality control ensures these binding/severing patterns are consistently observed by SDS-PAGE analysis.