Analytical Data
-
Gene name
Cofilin-2
- Application
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y281
-
Expression Region
Met1~Asn156
-
Molecular Weight
22kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Cofilin-2 is a member of the cofilin family of actin-binding proteins, which play a crucial role in the regulation of actin dynamics within cells. Actin is a fundamental component of the cytoskeleton, influencing cell shape, motility, and division. Cofilin-2 specifically is predominantly expressed in muscle tissues and has been implicated in various cellular processes, such as filament disassembly, recycling of actin monomers, and regulation of cell morphology. Research indicates that cofilin-2 is involved in muscle development and regeneration, and its dysregulation is associated with several pathologies, including muscular dystrophies and certain types of cancer. Consequently, understanding the functional mechanisms of cofilin-2 through recombinant protein studies is critical for elucidating its role in actin dynamics and muscle-related diseases. These studies facilitate insights into how cofilin-2 interacts with actin filaments, the impact of post-translational modifications, and potential therapeutic targets for muscle disorders. Exploring the biochemical and biophysical properties of recombinant cofilin-2 will enhance our knowledge of its regulatory functions and contribute to the development of novel strategies for treating diseases linked to actin cytoskeleton abnormalities. Thus, the study of cofilin-2 recombinant protein presents an important frontier in cellular biology and therapeutic research.
