NCEH1 Human

Neutral Cholesterol Ester Hydrolase 1 Human Recombinant
Cat. No.
BT27945
Source
E.coli.
Synonyms
AADACL1, NCEH, Neutral cholesterol ester hydrolase 1, Arylacetamide deacetylase-like, KIAA1363, NCEH1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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

NCEH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275a.a) and having a molecular mass of 33.6kDa. NCEH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neutral cholesterol ester hydrolase 1 (NCEH1) is an enzyme that plays a role in several biological processes. It hydrolyzes 2-acetyl monoalkylglycerol ether, a precursor in the production of platelet-activating factor. NCEH1 is involved in cholesterol ester hydrolysis within macrophages, contributing to atherosclerosis development. Additionally, it promotes tumor cell migration, playing a role in cancer progression. NCEH1 also participates in organ detoxification by breaking down organophosphorus compounds.
Description
Recombinant NCEH1, derived from humans and produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 298 amino acids (specifically, amino acids 1 through 275 with an added sequence) and has a molecular weight of 33.6 kDa. A 23 amino acid His-tag is fused to the N-terminus of the NCEH1 protein. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
The product is a clear and colorless solution that has been sterilized through filtration.
Formulation
This NCEH1 protein solution has a concentration of 1 mg/ml. It is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 0.4M urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be kept at 4°C. For extended storage, freezing at -20°C is recommended. Adding a carrier protein like HSA or BSA (0.1%) is beneficial for long-term storage. Avoid repeated freezing and thawing of the product.
Purity
The purity of the NCEH1 protein is determined to be greater than 90% using SDS-PAGE analysis.
Synonyms
AADACL1, NCEH, Neutral cholesterol ester hydrolase 1, Arylacetamide deacetylase-like, KIAA1363, NCEH1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEELNA VIVSIEYRLV PKVYFPEQIH DVVRATKYFL KPEVLQKYMV DPGRICISGD SAGGNLAAAL GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT PILPRYVMVK YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA AVRARLNWTS LLPASFTKNY KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL RDDGIMYAKR LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY IKWLDQNL.

Product Science Overview

Gene and Protein Structure

The NCEH1 gene is located on chromosome 3q26.31 in humans . The enzyme itself is a member of the serine hydrolase family and exhibits carboxylic ester hydrolase activity . It is involved in the hydrolysis of 2-acetyl monoalkylglycerol ether, a precursor in the synthesis of platelet-activating factor and lysophospholipids .

Biological Functions

NCEH1 is responsible for the hydrolysis of cholesterol esters in macrophages, contributing to the regulation of cholesterol homeostasis and the development of atherosclerosis . The enzyme also plays a role in the metabolism of xenobiotics and low-density lipoprotein (LDL) particle clearance .

Clinical Significance

Research has shown that NCEH1 is highly expressed in certain cancer cell lines, suggesting a potential role in cancer development . Reduction of NCEH1 levels in cancer cells has been associated with decreased tumor migration and growth in mice . Additionally, NCEH1 can hydrolyze organophosphates, such as the pesticide metabolite chlorpyrifos oxon .

Recombinant NCEH1

Recombinant NCEH1 is produced using recombinant DNA technology, which involves inserting the NCEH1 gene into a suitable expression system, such as bacteria or yeast, to produce the enzyme in large quantities. This recombinant enzyme is used in various research applications to study its function and potential therapeutic uses.

Recent Research

Recent studies have highlighted the role of NCEH1 in endothelial function, particularly in the context of diabetes . Deficiency of NCEH1 has been shown to impair endothelial function in diet-induced diabetic mice, suggesting that NCEH1 may be a promising candidate for the prevention and treatment of vascular complications associated with diabetes .

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