EREG Human, His

Epiregulin Human Recombinant, His Tag
Cat. No.
BT22255
Source
Escherichia Coli.
Synonyms
Epiregulin, Proepiregulin, ER, ERP.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 80.0% 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

EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa.
EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Epiregulin, a member of the EGF family, acts as a ligand for EGFR and most ERBB (v-erb-b2 oncogene homolog) family tyrosine-kinase receptors. Primarily found in the placenta, peripheral blood leukocytes, and certain bladder, lung, kidney, and colon carcinomas, Epiregulin promotes the growth of keratinocytes, hepatocytes, fibroblasts, and vascular smooth muscle cells while inhibiting the growth of several tumor-derived epithelial cell lines. Synthesized initially as a glycosylated 19.0 kDa transmembrane precursor protein, Human Epiregulin undergoes proteolytic cleavage to produce a mature 6.0 kDa secreted sequence.
Description
Recombinant Human EREG, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 69 amino acids (63-108 a.a) with a molecular mass of 7.7 kDa. This EREG protein is fused to a 23 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The EREG protein solution is provided at a concentration of 0.5 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the EREG protein is greater than 80.0% as determined by SDS-PAGE analysis.
Synonyms
Epiregulin, Proepiregulin, ER, ERP.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

Product Science Overview

Introduction

Epiregulin (EREG) is a member of the epidermal growth factor (EGF) family, which plays a crucial role in various cellular processes, including proliferation, differentiation, and survival. Epiregulin functions as a ligand for the epidermal growth factor receptor (EGFR) and other members of the ERBB family of tyrosine-kinase receptors .

Structure and Production

Human recombinant epiregulin is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. The recombinant protein contains 69 amino acids (63-108 a.a) and has a molecular mass of approximately 7.7 kDa . It is fused to a 23 amino acid His-tag at the N-terminus, which facilitates purification using chromatographic techniques .

Physical and Chemical Properties

The recombinant epiregulin is provided as a sterile, filtered, colorless solution. It is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0) and 10% glycerol . The protein solution is stable when stored at 4°C for short-term use (2-4 weeks) and at -20°C for long-term storage. To prevent degradation, it is recommended to avoid multiple freeze-thaw cycles and to add a carrier protein (0.1% HSA or BSA) for extended storage .

Biological Functions

Epiregulin is expressed in various tissues, including the placenta and peripheral blood leukocytes. It is also found in specific carcinomas of the bladder, lung, kidney, and colon . Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts, and vascular smooth muscle cells. Interestingly, it inhibits the growth of several tumor-derived epithelial cell lines .

Mechanism of Action

Epiregulin binds to EGFR and other ERBB receptors, inducing receptor homodimerization or heterodimerization with other ERBB family members . This binding activates downstream signaling pathways, such as the ERK1/2 and PI3K/Akt pathways, which are involved in cell proliferation and survival .

Applications in Research

Due to its role in cellular processes and cancer, epiregulin is widely used in laboratory research. It is utilized to study cell signaling pathways, cancer biology, and the development of potential therapeutic agents targeting EGFR and ERBB receptors .

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