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View ProductsSize | |
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Brand | |
Product type |
Product name | Recombinant Human PIK3R5 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 21.29 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | AntibodySystem |
Host species | Escherichia coli (E.coli) |
Fragment Type | Ala666-Cys838 |
Aliases /Synonyms | PIK3R5, Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit, PI3-kinase regulatory subunit 5, PtdIns-3-kinase regulatory subunit, Phosphoinositide 3-kinase regulatory subunit 5, PtdIns-3-kinase p101, p101-PI3K, Protein FOAP-2, PI3-kinase p101 subunit |
Reference | YHK68701 |
Note | For research use only. |
Recombinant Human PIK3R5 Protein, also known as Phosphoinositide-3-kinase regulatory subunit 5, is a protein that plays a crucial role in regulating various cellular processes such as cell growth, proliferation, and survival. This protein is encoded by the PIK3R5 gene and is a member of the phosphoinositide 3-kinase (PI3K) family. Recombinant Human PIK3R5 Protein is produced through recombinant DNA technology, making it a highly pure and bioactive protein for use in research and therapeutic applications.
Recombinant Human PIK3R5 Protein is a 55 kDa protein that consists of 507 amino acids. It contains several domains, including an SH2 domain, an SH3 domain, and a C-terminal domain. The SH2 domain is responsible for binding to phosphorylated tyrosine residues, while the SH3 domain is involved in protein-protein interactions. The C-terminal domain is important for the regulation of PI3K activity.
Recombinant Human PIK3R5 Protein also has a pleckstrin homology (PH) domain, which is responsible for binding to phosphoinositides, specifically phosphatidylinositol (3,4,5)-trisphosphate (PIP3). This binding results in the recruitment and activation of PI3K, leading to the production of the second messenger, phosphatidylinositol 3,4,5-trisphosphate (PIP3).
The main function of Recombinant Human PIK3R5 Protein is to regulate the activity of PI3K. PI3K is a key enzyme involved in the PI3K/AKT signaling pathway, which is essential for cell growth, proliferation, and survival. Recombinant Human PIK3R5 Protein acts as a regulatory subunit of PI3K, controlling its activity and specificity. It binds to the catalytic subunit of PI3K, p110, and stabilizes its interaction with PIP3, leading to the activation of PI3K and subsequent downstream signaling.
In addition to its role in PI3K regulation, Recombinant Human PIK3R5 Protein also plays a role in other cellular processes, including cell migration, adhesion, and cytoskeletal rearrangement. It has been shown to interact with several other proteins, such as focal adhesion kinase (FAK), paxillin, and actin, suggesting its involvement in these processes.
Recombinant Human PIK3R5 Protein has a wide range of applications in both research and therapeutic settings. In research, it is commonly used as a tool to study the PI3K/AKT signaling pathway and its role in various cellular processes. It can also be used to investigate the function of PIK3R5 in different disease states, such as cancer and autoimmune diseases.
In therapeutic applications, Recombinant Human PIK3R5 Protein has shown potential as a target for drug development. Dysregulation of the PI3K/AKT signaling pathway has been implicated in various diseases, including cancer, diabetes, and cardiovascular diseases. By targeting Recombinant Human PIK3R5 Protein, it may be possible to modulate the activity of PI3K and potentially treat these diseases.
Recombinant Human PIK3R5 Protein is a vital protein involved in the regulation of the PI3K/AKT signaling pathway and various cellular processes. Its structure, activity, and applications make it a valuable tool for research and a potential target for drug development. With ongoing research,
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