HB-EGF Human

HB-EGF Human Recombinant
Cat. No.
BT4312
Source
Escherichia Coli.
Synonyms

HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% 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

HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa.

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 EGF family that binds to the EGF receptor, leading to the stimulation of cell proliferation in a variety of cell types including smooth muscle cells, fibroblasts, epithelial cells, and keratinocytes. HB-EGF is found in several cell types and tissues, including vascular endothelial cells, smooth muscle cells, macrophages, skeletal muscle, keratinocytes, and certain tumor cells. Unlike other EGF-like molecules, HB-EGF possesses the unique ability to bind to heparin sulfate proteoglycans, which may contribute to its enhanced mitogenic activity on smooth muscle cells compared to EGF.

Description

Recombinant human HB-EGF, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 87 amino acids with a molecular weight of 9.9 kDa.

Purification of HB-EGF is achieved through proprietary chromatographic techniques.

Physical Appearance
The product appears as a sterile, white, lyophilized (freeze-dried) powder.
Formulation

The protein was lyophilized from a solution containing 10 mM sodium phosphate (pH 7.5) at a concentration of 1 mg/ml.

Solubility
To reconstitute the lyophilized human HB-EGF, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized recombinant human HB-EGF remains stable at room temperature for up to 3 weeks. However, it is recommended to store the lyophilized product desiccated at temperatures below -18°C. After reconstitution, HB-EGF should be stored at 4°C for 2-7 days. For long-term storage, freezing at -18°C is advised. To enhance stability during long-term storage, consider adding a carrier protein such as HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles.
Purity

The purity of the product is determined using SDS-PAGE analysis and is greater than 95.0%.

Biological Activity

The biological activity of HB-EGF is measured by its ability to stimulate the proliferation of 3T3 cells. The ED50, defined as the concentration required to induce a half-maximal proliferative response, is in the range of 0.13-0.2 ng/ml. This corresponds to an estimated specific activity of 7.7 x 106 units/mg.

Synonyms

HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.

Source
Escherichia Coli.
Amino Acid Sequence

MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC

KYVKELRAPS CICHPGYHGE RCHGLSL.

Product Science Overview

Discovery and Historical Background

HB-EGF was discovered in 1991 by Higashiyama et al. in the conditioned medium of human macrophage-like cells . It was the fourth growth factor identified among the ligands that bind to the EGF receptor (EGFR/ErbB1) . Some key milestones in the study of HB-EGF include:

  • Identification as the diphtheria toxin receptor (DTR) in 1992 .
  • Establishment of HB-EGF-null mouse lines in 2003 .
  • Discovery of its role in EGFR transactivation and nuclear translocation .
Structure and Function

HB-EGF is synthesized as a precursor protein that undergoes ectodomain shedding to produce the soluble mature form . This mature form influences the mitogenicity and chemotactic factors for smooth muscle cells and fibroblasts . HB-EGF binds to and activates EGFR and ErbB4, leading to the formation of homo- and heterodimers, autophosphorylation of specific tyrosine residues, and subsequent intracellular signaling .

Biological Significance

HB-EGF plays a crucial role in various physiological and pathological processes:

  • Cell Proliferation: It promotes the proliferation of various cell types, including fibroblasts and smooth muscle cells .
  • Wound Healing: HB-EGF is involved in tissue repair and regeneration.
  • Cancer: It has been identified as a promising target for cancer therapy due to its role in cell proliferation and survival .
Recombinant HB-EGF

Recombinant HB-EGF is produced using expression systems such as baculovirus-infected insect cells . The recombinant protein is used in research to study its biological functions and potential therapeutic applications. It is available in different formulations, including carrier-free versions for specific applications .

Applications

Recombinant HB-EGF has several applications in research and medicine:

  • Cell Culture: It is used to promote cell proliferation in various cell culture systems .
  • Therapeutic Research: Studies are ongoing to explore its potential in wound healing and cancer therapy .
  • Biochemical Studies: It is used to study the signaling pathways and interactions with other proteins .

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