Recombinant Human Cofilin 2 Protein (His Tag)

Name: Recombinant Human Cofilin 2 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1371
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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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	HGNC: 1875 OMIM: 601443 KEGG: hsa:1073 STRING: 9606.ENSP00000298159 UniGene: Hs.180141
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

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
The secreted levels of the cofilin-2 protein in radioresistant NPC patients were significantly higher than those of radiosensitive cases. PMID: 29664897
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
The greatest levels of circulating miR-297 and miR-19b-3p with its common target CFL2 are associated with metastatic prostate cancer. PMID: 28091918
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
In primary tumours, both desmin and CFL2 expression predicted improved overall survival in multivariate analyses PMID: 24889065
Cofilin 2 phosphorylation and genetic overexpression plays a role in the pathogenesis of idiopathic dilated cardiomyopthay. PMID: 25814227
patients with severe nemaline myopathy should be screened for mutations in CFL2. PMID: 24610938
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
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
PHD2 affects cell migration and F-actin formation via RhoA/rho-associated kinase-dependent cofilin phosphorylation PMID: 20801873
FXa-mediated sustained cofilin inactivation leads to stabilization of actin filaments incompatible with migration PMID: 20347121
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
CFL2, encoding the actin-binding protein muscle cofilin-2, is mutated in two siblings with congenital myopathy. PMID: 17160903
Resting T cells from infected patients carry significantly higher levels of active cofilin. PMID: 18928553
MLP binds directly to CFL2 in human cardiac and skeletal muscles. PMID: 19752190

FAQs

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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.