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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human RBM24 Protein, N-His-SUMO & C-Strep |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 22.51 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 | Thr11-Lys91 |
Aliases /Synonyms | RNA-binding region-containing protein 6, RNA-binding protein 24, RNA-binding motif protein 24, RBM24, RNPC6 |
Reference | ARO-P11756 |
Note | For research use only. |
Recombinant Human RBM24 Protein, also known as RNA-binding motif protein 24, is a protein that is encoded by the RBM24 gene. This protein is a member of the RNA recognition motif (RRM) family and is involved in post-transcriptional regulation of gene expression. Recombinant Human RBM24 Protein is produced through recombinant DNA technology, making it a valuable tool in various fields of research and biotechnology.
The primary structure of Recombinant Human RBM24 Protein consists of 279 amino acids with a molecular weight of approximately 31.2 kDa. It contains one RRM domain, which is responsible for RNA binding, and a C-terminal region that is rich in arginine and serine residues. This unique structure allows Recombinant Human RBM24 Protein to interact with various RNA molecules and regulate their function.
The three-dimensional structure of Recombinant Human RBM24 Protein has been determined through X-ray crystallography and NMR spectroscopy. It adopts a beta-alpha-beta motif, with the RRM domain forming a beta-sheet and the C-terminal region forming an alpha-helix. This structure allows Recombinant Human RBM24 Protein to bind to specific RNA sequences and regulate their processing and translation.
Recombinant Human RBM24 Protein plays a crucial role in post-transcriptional regulation of gene expression. It binds to specific RNA molecules, including pre-mRNA, and regulates their splicing, polyadenylation, and translation. This activity is essential for the proper functioning of cells and is crucial in development and disease processes.
Studies have shown that Recombinant Human RBM24 Protein interacts with other proteins involved in RNA processing, such as splicing factors and poly(A) polymerases. This interaction allows for the coordinated regulation of RNA processing, ensuring the production of functional and stable RNA molecules.
Recombinant Human RBM24 Protein has various applications in research and biotechnology. Its ability to regulate RNA processing makes it a valuable tool in studying gene expression and its dysregulation in diseases such as cancer and heart disease.
One of the major applications of Recombinant Human RBM24 Protein is in the production of recombinant proteins. It can be used as an antigen in protein expression systems to enhance the production and stability of recombinant proteins. This is due to its ability to bind to specific RNA sequences and regulate their translation, resulting in increased protein production.
Additionally, Recombinant Human RBM24 Protein has been used in the development of diagnostic assays for diseases such as leukemia and breast cancer. Its specific interaction with RNA molecules associated with these diseases makes it a valuable biomarker for their detection and monitoring.
In summary, Recombinant Human RBM24 Protein is a crucial player in post-transcriptional regulation of gene expression. Its unique structure and activity make it a valuable tool in various fields of research and biotechnology. Further studies on this protein and its interactions with other RNA-binding proteins will provide a better understanding of its role in cellular processes and its potential as a therapeutic target for diseases.
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