Recombinant Human ITGB6, N-His

Description of Recombinant Human ITGB6, N-His

Introduction

Recombinant Human ITGB6 is a protein that plays a crucial role in cell adhesion and signaling. It is a member of the integrin family of proteins, which are transmembrane receptors involved in various cellular processes, including cell adhesion, migration, and differentiation. ITGB6 is a heterodimeric protein composed of an α subunit and a β subunit, with the α subunit being non-covalently bound to the β subunit. In this article, we will discuss the structure, activity, and application of Recombinant Human ITGB6.

Structure of Recombinant Human ITGB6

The ITGB6 gene is located on chromosome 2 in humans and encodes the β6 subunit of the integrin protein. The β6 subunit has a molecular weight of approximately 90 kDa and is composed of 788 amino acids. It contains a large extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain is responsible for binding to other proteins, while the cytoplasmic tail is involved in intracellular signaling.

The α subunit of ITGB6 is encoded by the ITGA6 gene and has a molecular weight of approximately 150 kDa. It is composed of 1141 amino acids and contains a large extracellular domain, a single transmembrane domain, and a long cytoplasmic tail. The extracellular domain of the α subunit is responsible for binding to ligands, while the cytoplasmic tail interacts with intracellular signaling molecules.

When the α and β subunits of ITGB6 come together, they form a heterodimeric structure that spans the cell membrane. This structure allows ITGB6 to interact with other proteins and molecules both inside and outside of the cell.

Activity of Recombinant Human ITGB6

ITGB6 is primarily known for its role in cell adhesion and signaling. It is expressed on the surface of various cell types, including epithelial cells, fibroblasts, and immune cells. ITGB6 binds to a specific ligand, called integrin αvβ6, which is present on the surface of other cells and extracellular matrix proteins.

The binding of ITGB6 to integrin αvβ6 triggers a signaling cascade within the cell, leading to changes in cell behavior. This can include cell migration, proliferation, and differentiation. ITGB6 is also involved in the activation of certain growth factors, such as transforming growth factor-β (TGF-β), which play important roles in tissue repair and wound healing.

In addition to its role in cell adhesion and signaling, ITGB6 has also been implicated in various diseases and conditions. For example, overexpression of ITGB6 has been observed in certain cancers, including pancreatic and breast cancer, and has been associated with tumor growth and metastasis. ITGB6 has also been linked to fibrosis, a condition characterized by excessive scarring and tissue damage.

Application of Recombinant Human ITGB6

The recombinant form of ITGB6 has been widely used in scientific research and drug development. Recombinant Human ITGB6 can be produced in various expression systems, such as bacteria, yeast, and mammalian cells, and can be purified to high levels of purity.

One of the main applications of recombinant ITGB6 is in studying its role in cell adhesion and signaling. Researchers can use recombinant ITGB6 to investigate the binding properties of the protein and its interactions with other molecules. This can provide valuable insights into the mechanisms underlying cell adhesion and signaling.

Recombinant Human ITGB6 has also been used in drug development, particularly in the development of anti-cancer therapies. By targeting ITGB6, researchers aim to disrupt the interactions between cancer cells and their surrounding environment, potentially inhibiting tumor growth and metastasis. Additionally, recombinant ITGB6 has been investigated as a potential therapeutic target for fibrosis and other diseases.

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