Recombinant Human CD156b/ADAM17, N-His

Description of Recombinant Human CD156b/ADAM17, N-His

Introduction

Recombinant Human CD156b, also known as ADAM17, is a transmembrane protein belonging to the ADAM (a disintegrin and metalloproteinase) family. It is involved in various cellular processes such as cell adhesion, migration, and signaling. Recombinant Human CD156b/ADAM17 is a genetically engineered version of this protein that has been produced in a laboratory setting for research and therapeutic purposes. In this article, we will discuss the structure, activity, and applications of this recombinant protein.

Structure of Recombinant Human CD156b/ADAM17

The human CD156b/ADAM17 gene is located on chromosome 2 and codes for a protein of 824 amino acids. The recombinant version of this protein is produced by inserting the gene into a suitable expression vector and introducing it into a host cell, typically a bacterial or mammalian cell. The resulting protein has the same amino acid sequence as the native protein, but with additional sequences added to facilitate purification and detection.

The structure of Recombinant Human CD156b/ADAM17 consists of several domains, including a prodomain, a metalloproteinase domain, a disintegrin domain, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and a cytoplasmic tail. The prodomain is responsible for regulating the activity of the metalloproteinase domain, which is the catalytic site of the protein. The disintegrin domain is involved in cell adhesion, while the cysteine-rich domain is important for protein-protein interactions. The EGF-like domain is responsible for binding to growth factors and other ligands, and the transmembrane domain anchors the protein to the cell membrane. The cytoplasmic tail is involved in intracellular signaling.

Activity of Recombinant Human CD156b/ADAM17

Recombinant Human CD156b/ADAM17 is a metalloproteinase that cleaves various substrates, including membrane-bound proteins, growth factors, and cytokines. This activity is crucial for processes such as cell proliferation, differentiation, and migration. The metalloproteinase domain of CD156b/ADAM17 is responsible for this activity, and it requires a zinc ion for its catalytic function. The activity of CD156b/ADAM17 is tightly regulated by its prodomain, which must be removed for the protein to become active.

In addition to its proteolytic activity, Recombinant Human CD156b/ADAM17 also plays a role in cell adhesion. The disintegrin domain of the protein binds to integrins, which are transmembrane proteins involved in cell-cell and cell-matrix interactions. By binding to integrins, CD156b/ADAM17 can regulate cell adhesion and migration.

Applications of Recombinant Human CD156b/ADAM17

Recombinant Human CD156b/ADAM17 has a wide range of applications in both research and therapeutic settings. In research, this protein is commonly used as an antigen in studies investigating its role in various cellular processes. It can also be used as a tool to study the function of other proteins that interact with CD156b/ADAM17, such as growth factors and cytokines.

In the field of therapeutics, Recombinant Human CD156b/ADAM17 has shown potential as a target for cancer treatment. The overexpression of CD156b/ADAM17 has been observed in various types of cancer, and it is associated with tumor growth and metastasis. Inhibitors of CD156b/ADAM17 have been developed and are currently being tested in clinical trials as potential cancer therapies.

Furthermore, Recombinant Human CD156b/ADAM17 has been implicated in inflammatory diseases such as rheumatoid arthritis and psoriasis. Inhibiting its activity has been shown to reduce inflammation in animal models, making it a potential therapeutic target for these conditions.

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