EPGN Human, His

Epigen Human Recombinant, His Tag
Cat. No.
BT4763
Source
Escherichia Coli.
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.
EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Epidermal growth factor-like protein (EPGN) is a growth factor similar in structure to epidermal growth factor (EGF) that binds to and activates the ErbB receptor-1. EPGN is produced by various tissues, such as the testis, liver, heart, and certain tumor cells, and it promotes the proliferation of fibroblasts and epithelial cells. The human EPGN protein is initially synthesized as a glycosylated transmembrane precursor protein with a molecular weight of 14.7 kDa, which is then processed by proteolytic cleavage to generate a mature soluble form.
Description
Recombinant human EPGN, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 111 amino acids (residues 23-110) with a molecular weight of 12.1 kDa.
A 23 amino acid His-tag is fused to the N-terminus of the EPGN protein, which is purified using proprietary chromatographic methods.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
EPGN protein solution (1 mg/ml) in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M Urea.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C.
To ensure long-term stability, adding a carrier protein (0.1% HSA or BSA) is advisable.
Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is determined to be greater than 90.0% by SDS-PAGE analysis.
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

Product Science Overview

Identification and Structure

Epigen was identified through amino acid sequence homology with other EGF family members. The sequence was initially obtained from mouse keratinocyte mRNA . Human Epigen cDNA encodes a 154 amino acid residue type I transmembrane precursor glycoprotein. This glycoprotein consists of a 22 amino acid signal peptide, an 88 amino acid extracellular domain, a 21 amino acid transmembrane domain, and a 23 amino acid cytoplasmic domain .

Expression and Function

Epigen is expressed in normal human mammary tissue and in certain prostate and breast carcinomas . It binds to known EGF receptors, albeit with lower affinity compared to EGF. Despite this, Epigen is superior in inducing cell proliferation . It induces responses in MDA-MB-468 breast carcinoma cells and has effects on prostate cells and vascular endothelial cells . Epigen binds to ErbB1/Her1, causing receptor homodimerization and heterodimerization with other Erb/Her receptors .

Recombinant Production

Recombinant human Epigen (hEpigen) is produced in E. coli. The recombinant protein is typically purified to a high degree of purity, often greater than 98% as determined by SDS-PAGE . The bioactivity of recombinant hEpigen is measured in cell proliferation assays, with an ED50 typically between 2-30 ng/mL .

Applications

Recombinant Epigen is used in various research applications, particularly in studies related to cell proliferation and cancer research. It is important to note that products containing recombinant Epigen are labeled for research use only and are not approved for diagnostic or therapeutic purposes .

Epigen’s role in cell proliferation and its potential implications in cancer research make it a significant protein for further study and understanding.

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