CFL1 Human

Cofilin-1 Human Recombinant
Cat. No.
BT11230
Source
Escherichia Coli.
Synonyms
CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.
Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by Analysis by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Cofilin1 Human Recombinant (aa 1-166) fused to a 20 aa N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 186 amino acids and having a molecular mass of 20kDa.

Product Specs

Introduction
Cofilin belongs to a family of actin-binding proteins that play a crucial role in disassembling actin filaments. This widely distributed intracellular protein regulates actin dynamics by binding to and depolymerizing filamentous F-actin. Additionally, it inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Cofilin is involved in the cellular process of translocating the actin-cofilin complex from the cytoplasm to the nucleus.
Description
Recombinant Human Cofilin1 (amino acids 1-166) is expressed in E.Coli with an N-terminal 20 amino acid His-tag. This non-glycosylated polypeptide chain consists of 186 amino acids, resulting in a molecular weight of 20kDa.
Physical Appearance
The product is a sterile-filtered solution, appearing colorless.
Formulation
This protein solution is formulated in 20mM Tris buffer at pH 8.0 and contains 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of this protein is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCLSEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLVFIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL.

Product Science Overview

Structure and Function

Cofilin-1 is a small protein with a molecular weight of approximately 21 kDa . It binds to both monomeric (G-actin) and filamentous (F-actin) actin in a pH-dependent manner. At lower pH levels, cofilin-1 binds to F-actin, while at higher pH levels, it severs actin filaments and binds to G-actin . This dynamic binding and severing activity is essential for the reorganization of the actin cytoskeleton in response to various cellular signals .

Regulation

The activity of cofilin-1 is tightly regulated by several mechanisms, including phosphorylation, pH changes, and interactions with phosphoinositides . Phosphorylation of cofilin-1 at serine 3 by LIM kinase (LIMK) inhibits its actin-binding activity, while dephosphorylation by slingshot phosphatase (SSH) restores its activity . This regulation ensures that cofilin-1 activity is precisely controlled in response to cellular needs.

Recombinant Production

Human recombinant cofilin-1 is produced using bacterial expression systems. The recombinant protein is typically purified using ion exchange chromatography to achieve high purity levels (approximately 95%) . The recombinant form is often supplied as a lyophilized powder, which can be reconstituted in a suitable buffer for experimental use .

Biological Activity

The biological activity of recombinant cofilin-1 is assessed by its ability to bind and sever F-actin in a pH-dependent manner. Standard assays involve monitoring the actin-binding and severing activity of cofilin-1 using SDS-PAGE analysis of F-actin/cofilin spin-down assays performed at different pH levels . These assays ensure that the recombinant protein retains its functional properties.

Clinical Significance

Cofilin-1 is implicated in various physiological and pathological processes. It plays a vital role in cancer cell migration and invasion, particularly in colorectal cancer and esophageal squamous cell carcinoma . The differential expression of cofilin-1 and its regulators, such as LIMK1 and SSH1, is associated with tumor progression and metastasis . Understanding the role of cofilin-1 in these processes can provide insights into potential therapeutic targets for cancer treatment.

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