Ecotin E.Coli

Ecotin E.Coli Recombinant
Cat. No.
BT23826
Source
Escherichia Coli.
Synonyms

E. coli serine protease inhibitor.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTeks 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

Ecotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (21-162a.a.) and having a molecular mass of 18.3kDa.
Ecotin is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ecotin is a potent inhibitor of various pancreatic serine proteases, including chymotrypsin, trypsin, elastases, factor X, and kallikrein. Its inhibitory action is not restricted to a specific protease specificity.
Description
Produced in E. coli, our Ecotin is a non-glycosylated polypeptide chain consisting of 163 amino acids (21-162a.a.) with a molecular weight of 18.3 kDa. It features a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
The Ecotin protein is supplied at a concentration of 1 mg/ml in a buffer composed of 20mM Tris-HCl (pH 8.0), 1mM DTT, 50mM NaCl, and 10% glycerol.
Purity
Purity exceeding 95% as assessed by SDS-PAGE.
Stability
For optimal storage, refrigerate at 4°C if the entire vial will be consumed within 2-4 weeks. For extended storage, freeze at -20°C. Repeated freeze-thaw cycles should be avoided.
Synonyms

E. coli serine protease inhibitor.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MAESVQPLEK IAPYPQAEKG MKRQVIQLTP QEDESTLKVE LLIGQTLEVD CNLHRLGGKL ENKTLEGWGY DYYVFDKVSS PVSTMMACPD GKKEKKFVTA YLGDAGMLRY NSKLPIVVYT PDNVDVKYRV WKAEEKIDNA VVR

Product Science Overview

Structure and Function

Ecotin is a 16 kDa protein that consists of a monomer including a 20 amino acid signal peptide, which targets the protein to the periplasmic space of the bacterial cell . This protein inhibits various serine proteases such as chymotrypsin, trypsin, elastases, factor X, and kallikrein . The inhibition mechanism involves the interaction of ecotin with the protease, leading to the formation of a noncovalent complex that effectively traps the protease .

Biological Role

In E. coli, ecotin plays a crucial role in protecting the cell against host proteases. It is translocated to the periplasmic space, where it can protect the cell against neutrophil elastase (NE) that may have permeated through the damaged outer cell membrane of Gram-negative bacteria . This protective function is vital for the survival of the bacteria in hostile environments.

Recombinant Production

Recombinant production of ecotin in E. coli involves the use of genetic engineering techniques to express the ecotin gene in a host E. coli strain. This process allows for the production of large quantities of ecotin for research and industrial applications . The recombinant ecotin is typically directed to the periplasmic space, where it can fold properly and perform its inhibitory functions .

Applications

Ecotin has several applications in biotechnology and research. Its ability to inhibit a wide range of serine proteases makes it a valuable tool for studying protease functions and for developing protease inhibitors as therapeutic agents . Additionally, ecotin can be used in the production of recombinant proteins, where it helps in maintaining the solubility and stability of the target proteins .

In summary, ecotin is a versatile and potent serine protease inhibitor with significant biological and industrial importance. Its recombinant production in E. coli has opened up new avenues for research and applications in various fields.

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