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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
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 | Arovia |
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 | ARO-P11841 |
Note | For research use only. |
Recombinant Human PIK3R5 Protein, also known as Phosphoinositide-3-Kinase Regulatory Subunit 5, is a protein that is encoded by the PIK3R5 gene. It is a member of the phosphoinositide-3-kinase (PI3K) family, which plays a crucial role in cell signaling and regulation of various cellular processes. The protein is composed of 610 amino acids and has a molecular weight of approximately 70 kDa.
The primary structure of Recombinant Human PIK3R5 Protein includes an N-terminal SH2 domain, two proline-rich regions, and a C-terminal domain. The SH2 domain is responsible for binding to phosphorylated tyrosine residues on other proteins, thereby regulating the activity of PI3K. The proline-rich regions are involved in protein-protein interactions, while the C-terminal domain is important for the recruitment of the PI3K catalytic subunits.
In terms of secondary structure, Recombinant Human PIK3R5 Protein is predominantly composed of alpha-helices and beta-strands. The SH2 domain contains a three-stranded beta-sheet and two alpha-helices, while the C-terminal domain consists of a five-stranded beta-sheet and several alpha-helices. These structural elements are essential for the proper functioning of the protein.
Recombinant Human PIK3R5 Protein is a regulatory subunit of PI3K, which is an enzyme that catalyzes the phosphorylation of phosphatidylinositol lipids. This process results in the production of second messenger molecules that play a crucial role in various cellular processes, including cell growth, survival, and metabolism.
The activity of Recombinant Human PIK3R5 Protein is tightly regulated by various mechanisms. One of the key regulators is the binding of the SH2 domain to phosphorylated tyrosine residues on other proteins. This interaction leads to the activation of PI3K and subsequent downstream signaling events.
Moreover, Recombinant Human PIK3R5 Protein has been shown to play a role in the regulation of immune responses. It has been reported that the protein is involved in the activation of T cells and the production of pro-inflammatory cytokines. It also plays a role in the activation of B cells and the production of antibodies.
Recombinant Human PIK3R5 Protein has a wide range of applications in both basic research and clinical settings. In basic research, the protein is used to study the signaling pathways involved in various cellular processes. It is also used to investigate the role of PI3K in diseases such as cancer, diabetes, and autoimmune disorders.
In a clinical setting, Recombinant Human PIK3R5 Protein has potential therapeutic applications. As PI3K is often dysregulated in cancer, targeting this pathway with PI3K inhibitors, including Recombinant Human PIK3R5 Protein, has shown promising results in pre-clinical studies. Additionally, the protein has been studied for its potential use in the treatment of autoimmune diseases, such as multiple sclerosis and rheumatoid arthritis.
In conclusion, Recombinant Human PIK3R5 Protein is a crucial component of the PI3K signaling pathway, and its structure and activity play a vital role in regulating various cellular processes. Its potential therapeutic applications make it a valuable tool for both basic research and clinical studies.
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