Recombinant Human Cofilin 2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1371

Recombinant Human Cofilin 2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1371
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Product Overview

Tag His
Host Species Human
Accession Q9Y281
Synonym NEM7
Background Cofilin 2 (muscle), also known as CFL2, is a member of cofilin family of the actin-binding protein superfamily. Cofilin2 shows significant homology to the other two members: cofilin 1 and DSTN, through its entire sequence, and contains residues conserved among the cofilin family that are responsible for actin-binding. Cofilin 2 (CFL2) is an important regulator of striated myocyte function. Purified cofilin 2 depolymerized actin filaments in a dose- and pH-dependent manner and reduced the apparent viscosity of an actin solution, although they did not co-sediment with actin filaments at all. Cofilin2 is not expressed in vegetative cells, but is transiently induced during the aggregation stage of development, whereas cofilin 1 was predominantly expressed in vegetative cells.
Description A DNA sequence encoding the human CFL2 (Q9Y281-1) (Ala 2-Leu 166) was expressed, with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Ala 2-Leu 166
Molecular Weight The recombinant human CFL2 consisting of 180 a.a. and has a calculated molecular mass of 20.4 kDa. The apparent molecular mass of the protein is approximately 21 kDa in SDS-PAGE under reducing conditions.
Purity >98% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere.
Subcellular Location Nucleus matrix. Cytoplasm, cytoskeleton.
Protein Families Actin-binding proteins ADF family
Database References
Associated Diseases Nemaline myopathy 7 (NEM7)
Tissue Specificity Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues.

Gene Functions References

  1. Here we report atomic-level characterization by magic angle spinning (MAS) NMR of the muscle isoform of human cofilin 2 (CFL2) bound to F-actin. We demonstrate that resonance assignments for the majority of atoms are readily accomplished and we derive the intermolecular interface between CFL2 and F-actin. PMID: 28303963
  2. The secreted levels of the cofilin-2 protein in radioresistant NPC patients were significantly higher than those of radiosensitive cases. PMID: 29664897
  3. miR-3189-3p mimics enhanced the effects of the S100A4 siRNA on the inhibition of gastric cancer cell proliferation and migration by targeting CFL2. PMID: 29342841
  4. The greatest levels of circulating miR-297 and miR-19b-3p with its common target CFL2 are associated with metastatic prostate cancer. PMID: 28091918
  5. The serum lever of Alzheimer's disease were increase and the expression of clf2 strongly correlated with the Mini-Mental State Examination scores of the AD patients PMID: 25502766
  6. In primary tumours, both desmin and CFL2 expression predicted improved overall survival in multivariate analyses PMID: 24889065
  7. Cofilin 2 phosphorylation and genetic overexpression plays a role in the pathogenesis of idiopathic dilated cardiomyopthay. PMID: 25814227
  8. patients with severe nemaline myopathy should be screened for mutations in CFL2. PMID: 24610938
  9. A novel homozygous missense mutation in exon 2 (c.19G>A, p.Val7Met) of CFL2 was identified in two siblings with congenital myopathy. PMID: 22560515
  10. the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state PMID: 22158895
  11. PHD2 affects cell migration and F-actin formation via RhoA/rho-associated kinase-dependent cofilin phosphorylation PMID: 20801873
  12. FXa-mediated sustained cofilin inactivation leads to stabilization of actin filaments incompatible with migration PMID: 20347121
  13. actin depolymerizing factor/cofilins play an active role in establishing new interprotomer interfaces in F-actin that substitute for disrupted or weakened (as in ADP-actin) longitudinal contacts in filaments PMID: 16530787
  14. CFL2, encoding the actin-binding protein muscle cofilin-2, is mutated in two siblings with congenital myopathy. PMID: 17160903
  15. Resting T cells from infected patients carry significantly higher levels of active cofilin. PMID: 18928553
  16. MLP binds directly to CFL2 in human cardiac and skeletal muscles. PMID: 19752190


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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