Recombinant Human HBEGF, N-His

Reference: YHJ42901
Product nameRecombinant Human HBEGF, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight17.95 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeVal21-Thr160
Aliases /SynonymsDTR, DT-R, DTS, HEGFL, HB-EGF, HBEGF, Proheparin-binding EGF-like growth factor, Diphtheria toxin receptor
ReferenceYHJ42901
NoteFor research use only.

Description of Recombinant Human HBEGF, N-His

Introduction

Recombinant Human HBEGF, also known as heparin-binding EGF-like growth factor, is a protein that plays a crucial role in cell growth, proliferation, and differentiation. It is a member of the epidermal growth factor (EGF) family and is produced through recombinant DNA technology. In this article, we will discuss the structure, activity, and application of Recombinant Human HBEGF.

Structure of Recombinant Human HBEGF

Recombinant Human HBEGF is a 22 kDa protein consisting of 148 amino acids. It contains a single EGF-like domain, a heparin-binding domain, and a transmembrane domain. The EGF-like domain is responsible for binding to the EGF receptor (EGFR) and activating downstream signaling pathways. The heparin-binding domain allows the protein to bind to heparin sulfate proteoglycans on the cell surface, facilitating its interaction with the EGFR. The transmembrane domain anchors the protein to the cell membrane. Recombinant Human HBEGF is glycosylated, meaning it has sugar molecules attached to it, which can affect its stability and activity.

Activity of Recombinant Human HBEGF

Recombinant Human HBEGF is a potent mitogen, meaning it stimulates cell growth and division. It does so by binding to the EGFR and activating signaling pathways such as the MAPK and PI3K pathways. These pathways regulate various cellular processes such as cell proliferation, survival, and differentiation. Recombinant Human HBEGF has also been shown to promote wound healing by stimulating the migration and proliferation of epithelial cells. In addition, it has anti-apoptotic effects, protecting cells from programmed cell death. The activity of Recombinant Human HBEGF is tightly regulated to maintain normal cellular functions, and dysregulation of its activity has been linked to various diseases.

Application of Recombinant Human HBEGF

Recombinant Human HBEGF has a wide range of applications in both research and clinical settings. In research, it is commonly used as a tool to study the role of HBEGF in various cellular processes. It can be used to stimulate cell growth or wound healing in cell cultures or animal models. In addition, it can be used to investigate the signaling pathways activated by HBEGF and their downstream effects. Recombinant Human HBEGF is also used in drug discovery and development, as it is a potential target for therapeutic intervention in diseases such as cancer and cardiovascular diseases.

In the clinic, Recombinant Human HBEGF has been studied for its potential use in wound healing and tissue regeneration. It has been shown to promote wound healing in animal models and is currently being investigated for its potential use in diabetic foot ulcers and other chronic wounds. In addition, Recombinant Human HBEGF has been studied for its potential use in cardiovascular diseases, as it has been shown to have protective effects on the heart and blood vessels.

Conclusion

Recombinant Human HBEGF is a highly versatile protein with important roles in cell growth, proliferation, and differentiation. Its structure, activity, and applications make it a valuable tool in both research and clinical settings. Further studies on the regulation and function of Recombinant Human HBEGF may lead to new insights and potential therapeutic interventions for various diseases.

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