TWF1 Human

Twinfilin-1 Human Recombinant
Cat. No.
BT27649
Source
E.coli.
Synonyms
Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 80% as determined 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.
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Description

TWF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-252 a.a.) and having a molecular mass of 31.5kDa.
TWF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Twinfilin (TWF1), a protein found in all tissues, plays a crucial role in regulating the dynamics of actin, a protein essential for cell shape and movement. Composed of two similar regions called ADF-homology domains, TWF1 binds to individual actin molecules (actin monomers), specifically those bound to ADP. This binding prevents the exchange of ADP for ATP on the actin monomer, a process necessary for actin to form long chains called filaments. Consequently, TWF1 restricts the availability of actin monomers for filament assembly. The protein's structure comprises two ADF-H domains connected by a short linker region, followed by a tail region of about 20 amino acids. These ADF-H domains share approximately 20% similarity with each other and with related proteins like ADF/cofilin. Studies suggest that TWF1's ability to localize to specific cell regions enriched in actin monomers might be influenced by a small regulatory protein called RAC1.
Description
This product is a recombinant human TWF1 protein produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain comprising 277 amino acids (specifically, amino acids 1 to 252 of the TWF1 sequence) and has a molecular weight of 31.5kDa. This protein includes a 25 amino acid His-tag attached to its N-terminus and has been purified using specialized chromatographic methods.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
This solution contains TWF1 protein at a concentration of 0.25mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 40% glycerol, 0.15M NaCl, and 1mM DTT.
Stability
For short-term storage (up to 4 weeks), keep refrigerated at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein like HSA or BSA to a final concentration of 0.1% is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity of this product exceeds 80%, as determined by SDS-PAGE analysis.
Synonyms
Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMMLYAA TRATLKKEFG GGHIKDEVFG TVKEDVSLHG YKKYLLSQSS PAPLTAAEEE LRQIKINEVQ TDVGVDTKHQ TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD.

Product Science Overview

Introduction

Twinfilin-1, also known as TWF1 or PTK9, is a highly conserved actin monomer-binding protein that plays a crucial role in regulating cytoskeletal dynamics across a wide range of organisms, from yeast to mammals . This protein is particularly significant in the context of cellular processes such as cell motility, shape, and division.

Structure and Function

Twinfilin-1 is composed of two actin-depolymerizing factor homology (ADF-H) domains, which are responsible for its ability to bind actin monomers. This binding is essential for the regulation of actin filament turnover, a process critical for maintaining the dynamic nature of the cytoskeleton. The protein’s structure allows it to interact with actin in a way that promotes the disassembly of actin filaments, thereby facilitating various cellular activities .

Expression and Purification

Recombinant Human Twinfilin-1 is typically expressed in systems such as Escherichia coli or Baculovirus-infected Sf9 cells. The protein is then purified to a high degree of purity, often exceeding 80% or 95%, making it suitable for various experimental applications, including SDS-PAGE and Western Blotting . The recombinant form of Twinfilin-1 retains the functional properties of the native protein, allowing researchers to study its role in cytoskeletal dynamics in a controlled environment.

Biological Significance

The biological significance of Twinfilin-1 lies in its ability to regulate actin dynamics, which is fundamental to numerous cellular processes. By controlling the assembly and disassembly of actin filaments, Twinfilin-1 ensures that cells can adapt their shape and movement in response to various stimuli. This regulation is vital for processes such as cell migration, which is essential for wound healing, immune responses, and development.

Research Applications

Recombinant Human Twinfilin-1 is widely used in research to study the mechanisms of actin regulation and cytoskeletal dynamics. Its high purity and functional integrity make it an invaluable tool for experiments aimed at understanding the molecular basis of cell motility and shape changes. Additionally, Twinfilin-1 is used in studies exploring the effects of mutations and other modifications on actin dynamics, providing insights into various diseases and developmental disorders.

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