Recombinant Human FBN1, N-His

Description of Recombinant Human FBN1, N-His

Introduction

Recombinant Human FBN1, N-His is a genetically engineered form of the human Fibrillin-1 (FBN1) protein that has been modified with an N-terminal histidine tag. This protein is a crucial component of the extracellular matrix and is responsible for the structural integrity of various tissues, including the skin, blood vessels, and connective tissues. In this article, we will discuss the structure, activity, and potential applications of Recombinant Human FBN1, N-His as a drug target.

Structure of Recombinant Human FBN1, N-His

The FBN1 gene is located on chromosome 15 and encodes for the Fibrillin-1 protein, which is composed of 2871 amino acids. Recombinant Human FBN1, N-His is a truncated form of this protein, consisting of the first 130 amino acids of the FBN1 sequence, followed by a histidine tag. This tag allows for easy purification and detection of the protein. The overall structure of Fibrillin-1 is characterized by multiple calcium-binding epidermal growth factor-like (cbEGF) domains, which are responsible for the protein’s ability to interact with other extracellular matrix components.

Activity of this protein

Fibrillin-1 plays a crucial role in the formation and maintenance of elastic fibers, which are essential for the elasticity and strength of various tissues. These fibers are composed of microfibrils, which are formed by the polymerization of Fibrillin-1 monomers. The cbEGF domains of Fibrillin-1 interact with other proteins, such as integrins and fibronectin, to form a complex network that provides structural support to tissues. Additionally, Fibrillin-1 also regulates the activity of transforming growth factor-beta (TGF-β), a key signaling molecule involved in tissue development and repair.

Potential Applications as a Drug Target

Recombinant Human FBN1, N-His has the potential to be used as a drug target for various diseases and conditions that involve defects in elastic fiber formation. For example, mutations in the FBN1 gene are associated with Marfan syndrome, a genetic disorder characterized by abnormalities in connective tissues and blood vessels. By targeting Fibrillin-1, it may be possible to correct the underlying defects in elastic fiber formation and improve the symptoms of this condition.

Furthermore, Fibrillin-1 has been shown to play a role in the progression of certain types of cancer, such as breast and lung cancer. In these cancers, Fibrillin-1 promotes tumor growth and metastasis by interacting with other proteins in the extracellular matrix. By targeting Fibrillin-1, it may be possible to inhibit these interactions and prevent the spread of cancer cells.

Conclusion

In summary, Recombinant Human FBN1, N-His is a genetically engineered form of the Fibrillin-1 protein that has been modified with an N-terminal histidine tag. This protein plays a crucial role in the formation and maintenance of elastic fibers and has the potential to be used as a drug target for various diseases and conditions. Further research and development of this protein may lead to new treatments for conditions such as Marfan syndrome and certain types of cancer.