ETNK2 Human

EthanolamineKinase 2 Human Recombinant
Cat. No.
BT9959
Source
Escherichia Coli.
Synonyms

Ethanolaminekinase-2

Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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

ETNK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 47.2kDa.
ETNK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
ETNK2, part of the ethanolamine kinase family, catalyzes the initial step of phosphatidylethanolamine (PtdEtn) biosynthesis through the cytidine diphosphate pathway.
Description
Recombinant human ETNK2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 409 amino acids (amino acids 1-386). It has a molecular weight of 47.2 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile filtered solution.
Formulation
The ETNK2 protein solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of phosphate-buffered saline (pH 7.4), 10% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the ETNK2 protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms

Ethanolaminekinase-2

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVPPSA PQPRASFHLR RHTPCPQCSW GMEEKAAASA SCREPPGPPR AAAVAYFGIS VDPDDILPGA LRLIQELRPH WKPEQVRTKR FTDGITNKLV ACYVEEDMQD CVLVRVYGER TELLVDRENE VRNFQLLRAH SCAPKLYCTF QNGLCYEYMQ GVALEPEHIR EPRLFRLIAL EMAKIHTIHA NGSLPKPILW HKMHNYFTLV KNEINPSLSA DVPKVEVLER ELAWLKEHLS QLESPVVFCH NDLLCKNIIY DSIKGHVRFI DYEYAGYNYQ AFDIGNHFNE FAGVNEVDYC LYPARETQLQ WLHYYLQAQK GMAVTPREVQ RLYVQVNKFA LASHFFWALW ALIQNQYSTI DFDFLRYAVI RFNQYFKVKP QASALEMPK.

Product Science Overview

Introduction

Ethanolamine Kinase 2 is encoded by the ETNK2 gene in humans. The enzyme is responsible for phosphorylating ethanolamine to form phosphoethanolamine, which is a precursor in the biosynthesis of phosphatidylethanolamine. Phosphatidylethanolamine is a major phospholipid found in biological membranes and is essential for maintaining membrane integrity and function .

Preparation Methods

Recombinant human ETNK2 can be produced using various expression systems. One common method involves the use of Escherichia coli (E. coli) as the host organism. The ETNK2 gene is cloned into an expression vector, which is then introduced into E. coli cells. The recombinant protein is expressed with an N-terminal His-tag, which facilitates its purification using affinity chromatography .

Another method involves the use of a wheat germ expression system. In this approach, the ETNK2 gene is cloned into a vector and expressed in vitro using wheat germ extract. The recombinant protein is then purified using standard protein purification techniques .

Chemical Reactions and Analysis

Ethanolamine Kinase 2 catalyzes the phosphorylation of ethanolamine to form phosphoethanolamine. This reaction is the first step in the CDP-ethanolamine pathway, which ultimately leads to the synthesis of phosphatidylethanolamine. The enzyme’s activity can be analyzed using various biochemical assays that measure the formation of phosphoethanolamine from ethanolamine .

The recombinant ETNK2 protein is often used in research to study its role in phospholipid biosynthesis and its potential implications in various diseases. It is important to note that the recombinant protein may not always retain its full enzymatic activity, and its functionality should be verified through appropriate assays .

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