DEAD (Asp-Glu-Ala-Asp) box polypeptide 53 (502-513)

DEAD (Asp-Glu-Ala-Asp) box polypeptide 53 (502-513) is a synthetic peptide fragment derived from the C-terminal region of the DDX53 protein, a member of the DEAD-box RNA helicase family. Characterized by its conserved Asp-Glu-Ala-Asp (DEAD) motif, this polypeptide segment is of significant interest in biochemical research due to its involvement in RNA metabolism and gene expression regulation. As a research-use peptide, it provides a valuable tool for dissecting the structure-function relationships of DEAD-box helicases, facilitating the study of protein-protein and protein-RNA interactions, and supporting the development of novel molecular probes for cellular and molecular biology applications.

Peptide interaction studies: As a defined sequence corresponding to a functionally relevant region of DDX53, this polypeptide is frequently utilized to probe protein-protein and protein-nucleic acid interactions. Researchers employ it in affinity assays, pull-down experiments, and surface plasmon resonance analyses to characterize the binding partners of DDX53 or to map interaction domains within the helicase family. Such studies are crucial for elucidating the molecular mechanisms underlying RNA remodeling and the assembly of ribonucleoprotein complexes.

Antibody production and validation: The defined epitope represented by the 502-513 fragment of DDX53 makes it an optimal antigen for raising sequence-specific antibodies. Polyclonal or monoclonal antibodies generated against this peptide can be applied in immunoblotting, immunoprecipitation, and immunofluorescence studies, allowing for the selective detection and localization of endogenous or recombinant DDX53 in complex biological samples. These applications are instrumental in advancing our understanding of DDX53's cellular distribution and functional dynamics.

Functional assays and mechanistic studies: Synthetic peptides corresponding to conserved motifs of DEAD-box helicases are often incorporated into in vitro assays to dissect the biochemical activities of these enzymes. The 502-513 segment may be used to competitively inhibit or modulate the activity of full-length DDX53 or related helicases, enabling researchers to parse the contributions of specific domains to ATPase or RNA unwinding functions. Such targeted investigations provide insight into the mechanistic basis of RNA metabolism and the regulation of gene expression at the post-transcriptional level.

Peptide array and mapping applications: Due to its defined sequence and relevance to a conserved functional motif, this peptide is suitable for inclusion in peptide array platforms. Arrays featuring the 502-513 fragment facilitate high-throughput screening of protein-ligand interactions, post-translational modification sites, or the identification of small molecule binders. These approaches are valuable for drug discovery efforts, functional annotation of protein domains, and the identification of regulatory networks involving DEAD-box proteins.

Structural and conformational analysis: The synthetic availability of this polypeptide fragment enables detailed biophysical studies aimed at understanding the secondary structure and conformational dynamics of DEAD-box helicase domains. Techniques such as circular dichroism spectroscopy, nuclear magnetic resonance, or crystallography can be employed to investigate the folding properties and interaction surfaces of the segment. These structural insights are essential for rational design of modulators and for advancing the broader field of RNA helicase research.

1. Identification, Localization in the Central Nervous System and Novel Myostimulatory Effect of Allatostatins in Tenebrio molitor Beetle

2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

3. Emu oil in combination with other active ingredients for treating skin imperfections

4. A possible role of tachykinin-related peptide on an immune system activity of mealworm beetle, Tenebrio molitor L

5. Exosomes-mediated Transfer of miR-125a/b in Cell-to-cell Communication: A Novel Mechanism of Genetic Exchange in the Intestinal Microenvironment