Recombinant Human CFL2 protein(Ala2-Leu166), His-tagged

• Cat.No.: CFL2-6905H
• Product Overview: Recombinant Human CFL2 (Q9Y281-1) (Ala 2-Leu 166) was expressed in E. coli, with a polyhistidine tag at the N-terminus.

Specification

• Species: Human
• Source: E.coli
• Tag: His
• Protein Length: 2-166 a.a.
• Form: Lyophilized from sterile PBS, pH 7.5. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human CFL2 consisting of 180 amino acids 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
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: CFL2 cofilin 2 (muscle) [ Homo sapiens ]
• Official Symbol: CFL2
• Synonyms: CFL2; cofilin 2 (muscle); cofilin-2; cofilin, muscle isoform; NEM7
• Gene ID: 1073
• mRNA Refseq: NM_001243645
• Protein Refseq: NP_001230574
• MIM: 601443
• UniProt ID: Q9Y281

Case Study

Case 1: Pignataro M, et al. Redox Biol. 2020

Cofilins are proteins that help manage actin structure, crucial for various cell functions. They're mostly regulated by phosphorylation at a specific spot, which helps keep muscle fibers stable. In heart conditions, altered cofilin can clump in heart tissue. Oxidative stress can change cofilin, leading to these clumps. We studied how the inactive form of cofilin-2 reacts to oxidative stress and found it forms fibrous structures linked by a specific bond. Sulfide ions can prevent these structures, hinting that Na2S might protect against heart damage.

Fig1. Direct oxidation/reduction of cofilin cysteines.

Fig2. Effect of oxidative stress on cofilin aggregation imaged by Atomic Force Microscopy.

Case 2: Nguyen MT, et al. BMB Rep. 2022

Muscle health depends on proper formation, and issues here can lead to muscle loss. MiR-141-3p, linked to situations like aging, impacts muscle formation by reducing CFL2, a key protein for actin structure. Boosting miR-141-3p in muscle cells makes them grow faster but slows down the development of muscle proteins, which messes with muscle building. This shows how miR-141-3p influences muscle regulation through the CFL2-YAP pathway.

Fig1. After 24 h, CFL2 protein expressions were determined by immunobloting.

Fig2. Quantitative analysis of the protein expressions for CFL2 and myogenic factors.

Application

Recombinant CFL2 protein is grabbing attention, especially for its role in muscle and nerve health. Part of the Cofilin family, CFL2 helps manage actin dynamics-essential for cell shape and movement. In muscles, it's key to keeping things running smoothly, and researchers are looking into its use for tackling muscle conditions like atrophy. But muscles aren't the only area of interest. CFL2 is also crucial for nerve cells, affecting how they grow and communicate. This protein could provide insights into tackling neurodegenerative diseases. Since we can make CFL2 in the lab, it allows for detailed studies to better understand its role in both muscles and nerves. Pharmaceutical companies are also eyeing CFL2 for new treatments. Its impact on cells makes it a candidate for regenerative medicine, potentially helping in tissue repair. In short, by studying Recombinant CFL2, we're opening up possibilities for treating a variety of health challenges.