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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human MATR3 Protein, N-His-SUMO |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 23.83 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 | Lys478-Val576 |
Aliases /Synonyms | Matrin-3, KIAA0723, MATR3 |
Reference | ARO-P12119 |
Note | For research use only. |
Recombinant Human MATR3 Protein is a highly purified and biologically active protein that is produced through recombinant DNA technology. This protein is a member of the matrin family and is involved in various cellular processes such as RNA metabolism, transcription, and DNA repair. In this article, we will discuss the structure, activity, and applications of this important recombinant protein.
The MATR3 gene encodes a protein of 1261 amino acids, with a molecular weight of approximately 130 kDa. The recombinant protein is produced in a prokaryotic expression system and has a His-tag at the N-terminus for purification purposes. The purified protein is a homodimer with each monomer consisting of several functional domains.
The N-terminal domain of MATR3 contains a bipartite nuclear localization signal, which is responsible for the protein’s nuclear localization. This domain also contains two RNA recognition motifs (RRMs) that are essential for RNA binding. The central domain of MATR3 is rich in glycine and arginine residues and is involved in protein-protein interactions. The C-terminal domain contains a zinc finger motif, which is crucial for DNA binding and transcriptional regulation.
Recombinant Human MATR3 Protein is a multifunctional protein that plays a critical role in various cellular processes. One of its main functions is in RNA metabolism, where it binds to and regulates the processing, splicing, and transport of RNA molecules. MATR3 also interacts with other proteins involved in RNA metabolism, such as RNA helicases and RNA polymerases, to regulate their activity.
In addition to its role in RNA metabolism, MATR3 is also involved in transcriptional regulation. It interacts with transcription factors and co-regulators to modulate gene expression. MATR3 also plays a role in DNA repair, where it is recruited to sites of DNA damage and aids in the repair process.
Given its diverse functions, Recombinant Human MATR3 Protein has a wide range of applications in both research and therapeutic settings. One of the main applications of this protein is in studying RNA metabolism and gene expression. Researchers can use recombinant MATR3 to study the role of this protein in various cellular processes and its interactions with other proteins.
In addition, recombinant MATR3 has potential therapeutic applications. Studies have shown that mutations in the MATR3 gene are associated with several diseases, including amyotrophic lateral sclerosis (ALS) and distal myopathy. Recombinant MATR3 can be used in drug discovery and development for these diseases, as well as for other conditions where MATR3 dysregulation is implicated.
Furthermore, recombinant MATR3 can be used as an antigen in diagnostic assays for diseases associated with MATR3 mutations. Its high purity and biological activity make it an ideal candidate for developing sensitive and specific diagnostic tests.
Recombinant Human MATR3 Protein is a highly purified and biologically active protein that plays a critical role in various cellular processes. Its structure, activity, and applications make it an essential tool for studying RNA metabolism, gene expression, and potential therapeutic targets. As research on this protein continues, its potential for diagnostic and therapeutic applications will only increase.
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