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 (Heparin-binding EGF-like growth factor) is a protein produced through genetic engineering techniques, making it a highly purified and biologically active form of the naturally occurring human protein. HBEGF is an important growth factor that plays a crucial role in various cellular processes, making it a valuable tool for research and therapeutic applications.

Structure of Recombinant Human HBEGF

Recombinant human HBEGF is a 22 kDa protein consisting of 148 amino acids. It belongs to the EGF family of proteins and has a similar structure to other members, with the presence of six conserved cysteine residues that form three disulfide bonds. HBEGF also contains a heparin-binding domain, which is essential for its interaction with cell surface receptors.

Activity of Recombinant Human HBEGF

Recombinant human HBEGF is a potent mitogen, meaning it stimulates cell growth and proliferation. It exerts its activity by binding to its cell surface receptors, namely EGFR (Epidermal Growth Factor Receptor) and ErbB4 (Erythroblastic Leukemia Viral Oncogene Homolog 4). This binding triggers a cascade of signaling events, leading to cell growth, survival, and differentiation.

In addition to its mitogenic activity, HBEGF also has angiogenic properties, promoting the growth of new blood vessels. This is important for tissue repair and regeneration, as well as in diseases such as cancer where new blood vessel formation is necessary for tumor growth and metastasis.

Applications of Recombinant Human HBEGF

Recombinant human HBEGF has a wide range of applications in both research and therapeutic settings.

Research Applications

As a potent growth factor, recombinant human HBEGF is commonly used in cell culture experiments to stimulate cell growth and proliferation. It is also used in studies investigating the role of growth factors in various cellular processes, such as wound healing, tissue repair, and cancer development.

HBEGF is also used in studies exploring the mechanisms of action of other growth factors, as it can activate similar signaling pathways and interact with common receptors.

Therapeutic Applications

Recombinant human HBEGF has shown promising results in preclinical studies as a potential therapeutic agent for various diseases.

In cardiovascular diseases, HBEGF has been shown to promote the growth of new blood vessels, making it a potential treatment for conditions such as ischemic heart disease and peripheral artery disease.

In dermatological conditions, HBEGF has been found to promote wound healing and tissue repair, making it a potential treatment for chronic wounds, burns, and skin ulcers.

HBEGF also has potential in cancer therapy, as it has been shown to promote tumor growth and metastasis. However, further research is needed to fully understand its role in cancer and develop targeted therapies.

Conclusion

Recombinant human HBEGF is a highly purified and biologically active form of the naturally occurring human protein. Its structure, activity, and various applications make it a valuable tool for research and a promising therapeutic agent for various diseases. As research in this field continues, the potential of HBEGF in both research and therapeutic settings will continue to expand.

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