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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human PIP5K1A Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 47.08 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 | Lys62-Lys452 |
Aliases /Synonyms | PIP5K1-alpha, PtdIns(4)P-5-kinase 1 alpha, Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha, PIP5KIalpha, 68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha, PIP5K1A, Phosphatidylinositol 4-phosphate 5-kinase type I alpha |
Reference | ARO-P11840 |
Note | For research use only. |
Recombinant Human PIP5K1A Protein, also known as Phosphatidylinositol-4-Phosphate 5-Kinase Type-1 Alpha (PIP5K1A), is a highly conserved enzyme that plays a crucial role in cellular signaling pathways. This protein is produced through recombinant DNA technology, making it a valuable tool for scientific research and drug development.
The PIP5K1A protein is a member of the phosphatidylinositol-4-phosphate 5-kinase family, which contains three isoforms (alpha, beta, and gamma). The human PIP5K1A gene is located on chromosome 1 and is composed of 22 exons. The protein itself is composed of 673 amino acids and has a molecular weight of approximately 76 kDa.
The PIP5K1A protein has a highly conserved catalytic domain, which is responsible for its enzymatic activity. It also contains a pleckstrin homology (PH) domain, which is involved in protein-protein interactions and membrane localization. Additionally, PIP5K1A has a C-terminal domain that is important for its regulation and subcellular localization.
PIP5K1A is a lipid kinase that catalyzes the phosphorylation of phosphatidylinositol-4-phosphate (PI4P) to produce phosphatidylinositol-4,5-bisphosphate (PIP2). This reaction is essential for the synthesis of PIP2, which is a key signaling molecule involved in various cellular processes such as cell growth, proliferation, and survival.
The activity of PIP5K1A is tightly regulated by various factors, including its subcellular localization, protein-protein interactions, and post-translational modifications. For example, the PH domain of PIP5K1A binds to phosphatidylinositol-4,5-bisphosphate (PIP2), which promotes its membrane localization and activity. Additionally, PIP5K1A can be activated by various signaling pathways, such as growth factor signaling, calcium signaling, and phospholipase C signaling.
Due to its crucial role in cellular signaling, PIP5K1A has been implicated in various diseases, including cancer, diabetes, and neurological disorders. Therefore, recombinant PIP5K1A protein has become a valuable tool for studying the function and regulation of this protein in different disease models.
One of the main applications of recombinant PIP5K1A protein is in drug discovery and development. By understanding the structure and activity of PIP5K1A, scientists can design and screen potential inhibitors or activators of this protein for therapeutic purposes. For example, PIP5K1A inhibitors have been shown to have anti-cancer effects by inhibiting cell proliferation and inducing cell death in cancer cells.
Recombinant PIP5K1A protein is also used in biochemical and cell-based assays to study the role of PIP5K1A in various signaling pathways. By overexpressing or knocking down PIP5K1A in cells, researchers can investigate its effects on cellular processes and identify potential downstream targets.
Furthermore, recombinant PIP5K1A protein can be used as an antigen in antibody production or as a standard in immunoassays for the detection and quantification of PIP5K1A levels in biological samples. This allows for the study of PIP5K1A expression and activity in different tissues and disease states.
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