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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human FXR1 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 22.12 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 | Met1-Ala173 |
Aliases /Synonyms | Fragile X mental retardation syndrome-related protein 1, hFXR1p, FXR1 |
Reference | ARO-P12372 |
Note | For research use only. |
Recombinant Human FXR1 Protein, also known as Fragile X-related protein 1, is a member of the fragile X mental retardation protein (FMRP) family. It is encoded by the FXR1 gene and is expressed in various tissues, including the brain, heart, and skeletal muscle. FXR1 protein is involved in multiple cellular processes, such as RNA binding, translation regulation, and cell signaling. In this article, we will delve into the structure, activity, and application of Recombinant Human FXR1 Protein.
Recombinant Human FXR1 Protein is a 70 kDa protein consisting of 632 amino acids. It contains several functional domains, including two RNA-binding domains (RBDs), a nuclear localization signal (NLS), and a proline-rich region. The RBDs are responsible for binding to specific RNA sequences, while the NLS allows the protein to enter the nucleus. The proline-rich region is involved in protein-protein interactions, which are crucial for the function of FXR1 protein.
Recombinant Human FXR1 Protein plays a crucial role in regulating gene expression at the post-transcriptional level. It binds to specific RNA sequences, such as G-quadruplex structures, and regulates their translation. It has been shown to interact with various RNA-binding proteins, including FMRP and Fragile X-related protein 2 (FXR2), forming a complex known as the FMRP/FXR1/FXR2 complex. This complex is involved in the transport and translation of target mRNAs, which are important for neuronal development and synaptic plasticity.
In addition to its role in RNA regulation, FXR1 protein has been found to be involved in cell signaling pathways. It interacts with several proteins, including the tumor suppressor protein p53, and regulates its activity. FXR1 protein has also been shown to play a role in cell proliferation and differentiation, suggesting its potential involvement in tumorigenesis and tissue development.
Recombinant Human FXR1 Protein has been widely used in research to study its role in various cellular processes. It has been shown to be essential for neuronal development and synaptic plasticity, making it a potential therapeutic target for neurological disorders. Mutations in the FXR1 gene have been linked to Fragile X-related disorders, such as Fragile X syndrome, making FXR1 protein a potential biomarker for these conditions.
The RNA-binding activity of FXR1 protein has also made it a valuable tool for studying RNA regulation. Recombinant Human FXR1 Protein has been used in studies to identify and characterize RNA targets, as well as to investigate the mechanisms of RNA translation regulation. Its involvement in cell signaling pathways also makes it a potential target for drug development in cancer and other diseases.
In conclusion, Recombinant Human FXR1 Protein is a multifunctional protein with crucial roles in RNA regulation and cell signaling. Its structural features and activity make it an important player in various cellular processes, making it a valuable tool for research and a potential therapeutic target for diseases. Further studies on FXR1 protein and its interactions with other proteins and RNA targets will provide a deeper understanding of its functions and potential applications.
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