HB-EGF Rat
Proheparin-Binding EGF-like Growth Factor Rat Recombinant
Cat. No.
BT4595
Source
Escherichia Coli.
Synonyms
Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis 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.
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Description
HB-EGF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.7kDa.
The HB-EGF is purified by proprietary chromatographic techniques.
The HB-EGF is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Heparin-binding EGF-like growth factor (HB-EGF) is a member of the epidermal growth factor (EGF) family that binds to and activates the EGF receptor (EGFR). HB-EGF promotes the growth of various cell types, including smooth muscle cells, fibroblasts, epithelial cells, and keratinocytes. It is produced by a variety of cells, including vascular endothelial cells, smooth muscle cells, macrophages, skeletal muscle cells, keratinocytes, and some tumor cells. Unlike other EGF-like molecules, HB-EGF can bind to heparin and heparan sulfate proteoglycans, which may contribute to its enhanced mitogenic activity on smooth muscle cells compared to EGF.
Description
Recombinant Rat HB-EGF is a single, non-glycosylated polypeptide chain containing 86 amino acids, with a molecular weight of 9.7 kDa. Produced in E. coli, it is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The protein solution was sterile filtered (0.2µm) and lyophilized from a concentrated solution in phosphate-buffered saline (PBS), 300mM NaCl at pH 7.4 containing 5% trehalose.
Solubility
Reconstitute the lyophilized Rat HB-EGF in sterile 18M-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Rat HB-EGF Recombinant is stable at room temperature for 3 weeks. However, for long-term storage, it is recommended to store desiccated below -18°C. After reconstitution, HB-EGF should be stored at 4°C for 2-7 days or below -18°C for future use. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 95.0% by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis. (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED50, determined by a cell proliferation assay using balb/c 3T3 cells, is less than 1.0 ng/ml. This corresponds to a specific activity of greater than 1.0 x 106 units/mg.
Synonyms
Proheparin-binding EGF-like growth factor, Heparin-binding EGF-like growth factor, HB-EGF, HBEGF, Dtr, Hegfl, GFHB.
Source
Escherichia Coli.
Amino Acid Sequence
DLEGTDLDLF KVAFSSKPQA LATPGKEKNG KKKRKGKGLG KKRDPCLKKY KDYCIHGECR YLKELRIPSC HCLPGYHGQR CHGLTL.
Product Science Overview
Structure and Function
HB-EGF is initially synthesized as a transmembrane precursor, which is then cleaved to release the soluble form. The soluble form of HB-EGF can bind to and activate the EGF receptor (EGFR) with higher affinity than EGF itself . This binding leads to the activation of several downstream signaling pathways, including the ERBB2 and ERBB4 pathways .
HB-EGF is known to play a crucial role in various physiological processes, such as:
- Cardiac Development: It is required for normal cardiac valve formation and heart function .
- Smooth Muscle Cell Proliferation: It promotes the proliferation of smooth muscle cells, which is essential for vascular development and repair .
- Wound Healing: HB-EGF is involved in the positive regulation of cell migration and proliferation, contributing to wound healing and tissue regeneration .
Biological Activities
HB-EGF exhibits several biological activities, including:
- Mitogenic Activity: It is a potent mitogen for fibroblasts and smooth muscle cells but not for endothelial cells .
- Chemotactic Activity: It acts as a chemotactic factor, attracting cells to the site of injury or inflammation .
- Receptor Binding: HB-EGF binds to the EGF receptor (EGFR) with higher affinity than EGF itself, making it a more potent activator of EGFR signaling pathways .
Clinical Implications
HB-EGF has been implicated in various clinical conditions and diseases:
- Cardiovascular Diseases: Due to its role in smooth muscle cell proliferation and cardiac development, HB-EGF is being studied for its potential therapeutic applications in cardiovascular diseases .
- Cancer: HB-EGF is overexpressed in several types of cancer, including breast, ovarian, and gastric cancers. Its ability to promote cell proliferation and migration makes it a potential target for cancer therapy .
- Wound Healing: The role of HB-EGF in wound healing and tissue regeneration has led to its investigation as a therapeutic agent for chronic wounds and other conditions requiring enhanced tissue repair .
Research Applications
The rat recombinant form of HB-EGF is widely used in research to study its biological functions and potential therapeutic applications. Researchers use this protein to investigate its role in various physiological and pathological processes, including:
- Cell Proliferation and Migration: Studies on HB-EGF help to understand its effects on cell proliferation and migration, which are crucial for tissue development and repair .
- Signal Transduction Pathways: Research on HB-EGF provides insights into the signaling pathways activated by its binding to EGFR and other receptors .
- Disease Models: The rat recombinant form of HB-EGF is used in animal models to study its role in diseases such as cancer, cardiovascular diseases, and wound healing .
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