Recombinant Human REEP1 Protein, N-His-SUMO & C-Strep from ProteoGenix; catalogue ARO-P11752; research use only.
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Recombinant Human REEP1 Protein is a highly purified and biologically active protein that is produced through genetic engineering techniques. It is a member of the REEP family of proteins, which are involved in the regulation of endoplasmic reticulum (ER) structure and function. This protein has been extensively studied and has shown promising results in various research areas, making it a valuable tool for scientists.
The Recombinant Human REEP1 Protein is a 22 kDa protein consisting of 197 amino acids. It is composed of a hydrophobic N-terminal transmembrane domain and a C-terminal cytoplasmic domain. The transmembrane domain is responsible for anchoring the protein to the ER membrane, while the cytoplasmic domain is involved in protein-protein interactions.
Recombinant Human REEP1 Protein has been shown to play a crucial role in maintaining the structure and function of the ER. It interacts with other proteins to form a network that regulates the shape and dynamics of the ER. This network is essential for the proper functioning of the ER, which is responsible for protein synthesis, folding, and transport.
Studies have also shown that REEP1 protein is involved in the formation of lipid droplets, which are important for lipid metabolism and energy storage. It has been suggested that REEP1 may play a role in the regulation of lipid droplet size and number.
Furthermore, Recombinant Human REEP1 Protein has been shown to play a role in neurodegenerative diseases such as hereditary spastic paraplegia (HSP). Mutations in the REEP1 gene have been linked to the development of HSP, and studies have shown that these mutations result in a loss of REEP1 protein function. This highlights the importance of REEP1 in maintaining the proper function of the nervous system.
Due to its crucial role in maintaining ER structure and function, Recombinant Human REEP1 Protein has a wide range of applications in scientific research. Some of the key areas where this protein has been used include:
As mentioned earlier, REEP1 protein has been linked to neurodegenerative diseases such as HSP. Therefore, it has been extensively studied in the field of neuroscience to understand its role in maintaining the structure and function of the nervous system. Recombinant Human REEP1 Protein has been used to study the effects of REEP1 mutations on neuronal function and to develop potential treatments for HSP.
The ER plays a crucial role in protein synthesis, folding, and transport, making it a key organelle in cell biology. Recombinant Human REEP1 Protein has been used to study the structure and function of the ER and its role in various cellular processes. It has also been used to investigate the role of REEP1 in lipid metabolism and lipid droplet formation.
Given the involvement of REEP1 in neurodegenerative diseases, Recombinant Human REEP1 Protein has been used in drug development studies. It has been used to screen potential drug candidates that can target REEP1 and potentially treat HSP and other related disorders.
Recombinant Human REEP1 Protein has also been used as a diagnostic tool to detect mutations in the REEP1 gene. This can aid in the early diagnosis of HSP and other neurodegenerative diseases, allowing for timely treatment and management.
In summary, Recombinant Human REEP1 Protein is a highly valuable tool in scientific research due to its crucial role in maintaining ER structure and function. Its applications in various fields such as neuroscience, cell biology, drug development, and diagnostics make it an important protein for
ProteoGenix catalogue number ARO-P11752. For research use only.
Host: Escherichia coli (E.coli); Expression system: Prokaryotic expression; Molecular weight: 25.58 kDa; Fragment: Asp56-Gly161; Buffer: Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol..
Available configurations: 50ug, 100ug, 1mg.
This product is manufactured by ProteoGenix and sold through ABMIUM without relabelling.
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