Recombinant Human DHX15 Protein, N-His

Reference: YHA57901
Product nameRecombinant Human DHX15 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight29.13 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°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)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeAsp568-Tyr795
Aliases /SynonymsDDX15, DEAH box protein 15, Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15, DHX15, DBP1, ATP-dependent RNA helicase #46
ReferenceYHA57901
NoteFor research use only.

Description of Recombinant Human DHX15 Protein, N-His

Introduction to Recombinant Human DHX15 Protein

Recombinant Human DHX15 Protein, also known as DExH-box helicase 15, is a highly conserved protein that plays a crucial role in RNA metabolism and processing. It is a member of the DEAD-box helicase family, which is characterized by the presence of a conserved Asp-Glu-Ala-Asp (DEAD) motif in the helicase domain. DHX15 is involved in various cellular processes such as RNA splicing, translation, and ribosome biogenesis, making it an essential protein for cell survival and function.

Structure of Recombinant Human DHX15 Protein

The human DHX15 gene is located on chromosome 1 and consists of 26 exons, which undergo alternative splicing to produce multiple isoforms of the protein. The full-length protein contains 1,369 amino acids and has a molecular weight of approximately 150 kDa. DHX15 has a highly conserved helicase domain, which is responsible for its ATP-dependent RNA helicase activity. It also contains an N-terminal DEAD-box domain and a C-terminal helicase-associated domain, both of which are essential for its function.

Structural studies have revealed that DHX15 adopts a ring-like structure, with the helicase domain forming the central core and the DEAD-box and helicase-associated domains protruding outwards. This unique structure allows DHX15 to interact with various RNA molecules and proteins, making it a versatile player in RNA metabolism.

Activity of Recombinant Human DHX15 Protein

As a DEAD-box helicase, DHX15 uses the energy from ATP hydrolysis to unwind RNA duplexes and displace proteins bound to RNA molecules. It has been shown to have a preference for single-stranded RNA with a 5′-triphosphate end, which is a common feature of newly synthesized RNA molecules. DHX15 is also involved in the release of ribosomal subunits during translation initiation and the remodeling of ribonucleoprotein complexes during RNA splicing.

In addition to its helicase activity, DHX15 also has ATPase activity, which is essential for its function. The ATPase activity of DHX15 is stimulated by RNA binding and is required for its helicase activity. This dual activity of DHX15 allows it to efficiently unwind and remodel RNA molecules, making it a critical component of various cellular processes.

Application of Recombinant Human DHX15 Protein

Recombinant Human DHX15 Protein has been widely used in research to study its role in various cellular processes. It has been shown to be essential for cell viability, as knockdown or inhibition of DHX15 leads to cell death. DHX15 has also been implicated in various diseases, including cancer, viral infections, and neurodegenerative disorders, making it a potential therapeutic target.

Furthermore, DHX15 has been used as a tool in RNA research, as its helicase activity can be harnessed to study RNA structure and function. It has also been used in the development of high-throughput screening assays for potential inhibitors of its activity, which could have therapeutic implications in diseases where DHX15 is dysregulated.

In conclusion, Recombinant Human DHX15 Protein is a highly conserved and versatile protein that plays a crucial role in RNA metabolism and processing. Its unique structure and dual activity make it an essential player in various cellular processes and a potential therapeutic target. With further research, DHX15 could provide valuable insights into the mechanisms of RNA regulation and contribute to the development of novel treatments for diseases where it is involved.

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