DSTN Human

Destrin Human Recombinant
Cat. No.
BT5459
Source
E.coli.
Synonyms
Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% 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.
Shipped with Ice Packs
In Stock

Description

DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.
DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Actin depolymerizing factor (Destrin/DSTN) is a protein that belongs to the ADF/Cofilin/destrin family. This family is known for its ability to rapidly depolymerize filamentous actin (F-Actin) in a stoichiometric manner. The ADF family plays a crucial role in regulating the turnover rate of actin within living cells. Destrin, specifically, is a small actin-binding protein sensitive to phosphoinositides and capable of depolymerizing actin filaments in laboratory settings. Its function is independent of pH. While present in various epithelial and endothelial cells, Destrin is largely absent in adult mouse heart and skeletal muscle cells. Although sharing a 71% sequence similarity with Cofilin, Destrin exhibits differences in its interaction with Actin.
Description
Recombinant human DSTN, produced in E. coli, is a single polypeptide chain consisting of 173 amino acids (residues 1-165) with a molecular weight of 19.5 kDa. It features an 8 amino acid His-tag fused at the C-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The DSTN solution is provided at a concentration of 0.5mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity is determined to be greater than 95% by SDS-PAGE analysis.
Synonyms
Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.
Source
E.coli.
Amino Acid Sequence
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH HHH

Product Science Overview

Structure and Function

Destrin is a small, phosphoinositide-sensitive actin-binding protein. It is composed of 165 amino acids and has a molecular weight of approximately 19.5 kDa . The protein is capable of depolymerizing actin filaments in vitro, which is crucial for various cellular processes such as cell motility, division, and maintenance of cell shape .

Expression and Localization

Destrin is found in various epithelial and endothelial cells but is practically absent from adult mouse heart and skeletal muscle cells . It shares 71% sequence homology with cofilin, another member of the same superfamily, but the two proteins differ in their interaction with actin .

Recombinant Production

Recombinant human destrin is typically produced in E. coli and purified using conventional chromatography techniques . The recombinant protein often includes a C-terminal His-tag to facilitate purification and detection . The protein is stored in a buffer containing Tris-HCl, NaCl, glycerol, and DTT to maintain its stability .

Applications

Recombinant destrin is used in various research applications, including studies on actin dynamics, cell motility, and cytoskeletal organization. It is also used to investigate the molecular mechanisms underlying actin filament depolymerization and the role of actin-binding proteins in cellular processes .

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