Recombinant Human EGFR/ERBB1/HER1 Protein, N-His

Description of Recombinant Human EGFR/ERBB1/HER1 Protein, N-His

Introduction

Recombinant Human EGFR/ERBB1/HER1 Protein, also known as Epidermal Growth Factor Receptor (EGFR), is a transmembrane protein that plays a crucial role in cell signaling and growth. It is a member of the ERBB family of receptor tyrosine kinases and is encoded by the ERBB1 gene. Recombinant Human EGFR/ERBB1/HER1 Protein is widely used in research and has various applications in the field of cancer biology and drug discovery.

Structure

Recombinant Human EGFR/ERBB1/HER1 Protein is composed of 1210 amino acids and has a molecular weight of approximately 170 kDa. It consists of an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain contains four subdomains, namely I-IV, which are responsible for ligand binding. The transmembrane domain anchors the protein to the cell membrane, and the intracellular domain contains the tyrosine kinase catalytic domain.

Activity

Recombinant Human EGFR/ERBB1/HER1 Protein is activated by binding to its ligands, such as epidermal growth factor (EGF) and transforming growth factor alpha (TGF-α). Upon ligand binding, the receptor undergoes a conformational change, leading to the activation of its tyrosine kinase activity. This results in the auto-phosphorylation of specific tyrosine residues in the intracellular domain, which serves as docking sites for downstream signaling molecules.

The activation of Recombinant Human EGFR/ERBB1/HER1 Protein triggers a cascade of signaling pathways, including the PI3K-AKT and MAPK-ERK pathways, which are involved in cell proliferation, survival, and differentiation. Abnormal activation of EGFR has been linked to various cancers, making it an important target for cancer therapy.

Application

Recombinant Human EGFR/ERBB1/HER1 Protein has several applications in the field of cancer research and drug discovery. It is commonly used as an antigen in the production of antibodies for studying EGFR signaling and its role in cancer. The protein can also be used in receptor-ligand binding assays to screen for potential inhibitors or activators of EGFR.

Recombinant Human EGFR/ERBB1/HER1 Protein has also been used in preclinical studies to test the efficacy of EGFR-targeted therapies, such as monoclonal antibodies and tyrosine kinase inhibitors. These therapies have shown promising results in the treatment of various cancers, including lung, breast, and colorectal cancer.

Furthermore, Recombinant Human EGFR/ERBB1/HER1 Protein has been used in structural studies to understand the mechanism of ligand binding and receptor activation. This information can aid in the development of more specific and potent EGFR inhibitors for cancer treatment.

Conclusion

Recombinant Human EGFR/ERBB1/HER1 Protein is a crucial protein in cell signaling and growth, with various applications in cancer research and drug discovery. Its well-defined structure and activity make it an ideal target for studying the mechanisms of cancer development and for developing targeted therapies. With ongoing research and advancements in technology, the potential of Recombinant Human EGFR/ERBB1/HER1 Protein in the field of cancer biology continues to expand.