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AntibodySystem
Recombinant Proteins
Recombinant Human RHBDL2 Protein, also known as RHBDF2, is a type II transmembrane protein that belongs to the rhomboid family of serine proteases. It is encoded by the RHBDF2 gene and is expressed in various tissues including the brain, heart, liver, and kidney. RHBDL2 is involved in the cleavage and release of membrane-bound proteins, making it an important player in various cellular processes. In this article, we will delve deeper into the structure, activity, and applications of this protein.
The gene for RHBDL2 is located on chromosome 17 and consists of 9 exons, which encode for a protein of 293 amino acids. The protein has a predicted molecular weight of approximately 32 kDa and contains a signal peptide, a transmembrane domain, and a catalytic domain. The signal peptide is responsible for directing the protein to the endoplasmic reticulum, where it undergoes post-translational modifications. The transmembrane domain anchors the protein to the cell membrane, while the catalytic domain contains the active site responsible for proteolytic activity.
RHBDL2 is a serine protease that is involved in the cleavage and release of membrane-bound proteins. It is known to cleave various substrates, including the amyloid precursor protein (APP), which is involved in the pathology of Alzheimer’s disease. RHBDL2 has also been shown to cleave the Notch receptor, a key regulator of cell differentiation and development. This proteolytic activity is essential for the proper functioning of these proteins and is tightly regulated to prevent any aberrant cleavage.
In addition to its role in proteolysis, RHBDL2 has been implicated in other cellular processes. It has been shown to play a role in the regulation of cell proliferation and migration, as well as in the maintenance of cell polarity. Furthermore, RHBDL2 has been found to interact with other proteins, such as the EGF receptor, and modulate their activity, highlighting its diverse functions in the cell.
The recombinant form of RHBDL2 has been widely used in various research applications. One of the main applications is in the study of the proteolytic activity of this protein. Recombinant RHBDL2 can be used to cleave specific substrates in vitro, providing valuable insights into its activity and regulation. This has been particularly useful in understanding the role of RHBDL2 in the cleavage of amyloid precursor protein and its potential implications in Alzheimer’s disease.
Moreover, recombinant RHBDL2 has been used in the production of monoclonal antibodies. The protein can be used as an antigen to elicit an immune response in animals, leading to the production of antibodies that can be used in various research and diagnostic applications. These antibodies can also be used to study the expression and localization of RHBDL2 in different tissues and cell types.
In addition, RHBDL2 has been identified as a potential therapeutic target in various diseases. For instance, the dysregulation of RHBDL2 has been linked to the progression of certain cancers, making it a potential target for cancer therapy. Furthermore, the role of RHBDL2 in the cleavage of Notch receptor has also sparked interest in its potential as a therapeutic target in diseases involving Notch signaling, such as cardiovascular diseases and developmental disorders.
In summary, Recombinant Human RHBDL2 Protein is a type II transmembrane protein that plays a crucial role in the cleavage and release of membrane-bound proteins. Its structure, activity, and diverse functions make it an important player in various cellular processes. The availability of recombinant RHBDL2 has greatly facilitated its study and has opened up new opportunities for its applications in research and therapeutics
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