Nuclear pore complex protein Nup98 (315-360) is the 315-360 fragment part of the nuclear pore complex (NPC) protein.
CAT No: R1570
Nuclear pore complex protein Nup98 315-360 is a synthetic peptide segment derived from the N-terminal region of the Nup98 nucleoporin, a critical component of the nuclear pore complex (NPC) in eukaryotic cells. This peptide encompasses amino acids 315 to 360 of the full-length Nup98 protein, a region known to participate in essential protein-protein interactions within the NPC and contribute to the regulation of nucleocytoplasmic transport. As a modular element of the Nup98 structure, the 315-360 fragment is of particular interest to researchers investigating the molecular architecture and functional dynamics of the nuclear pore, as well as those exploring the broader roles of nucleoporins in genome organization and cellular signaling.
Protein interaction studies: The Nup98 315-360 peptide is frequently utilized in in vitro binding assays, such as pull-down experiments or surface plasmon resonance analyses, to dissect the specific molecular interactions between Nup98 and its binding partners. By providing a defined segment of the protein, this peptide enables researchers to map interaction domains, characterize binding affinities, and elucidate the mechanistic basis for Nup98's recruitment to the NPC or its association with transport factors, transcriptional regulators, or chromatin-modifying complexes.
Nuclear transport mechanism research: As a functional domain implicated in nucleocytoplasmic trafficking, the 315-360 region of Nup98 serves as a valuable tool for studying transport selectivity, cargo recognition, and the dynamics of macromolecular translocation across the nuclear envelope. Researchers employ this peptide in reconstituted transport assays or as a competitive inhibitor to probe the role of specific Nup98 segments in mediating the passage of proteins and ribonucleoprotein complexes through the NPC, thereby advancing understanding of nuclear transport regulation.
Antibody generation and epitope mapping: The defined sequence of the Nup98 315-360 peptide makes it a suitable immunogen for the production of sequence-specific antibodies. Such antibodies are instrumental in applications ranging from immunoblotting and immunofluorescence to immunoprecipitation, enabling the detection, localization, and quantitation of Nup98 or its fragments in cellular and biochemical samples. Furthermore, the peptide can be used in epitope mapping studies to identify antibody binding sites and refine the specificity of immunological reagents targeting nucleoporins.
Structural and biophysical analyses: The isolated Nup98 315-360 segment is amenable to a range of structural biology techniques, including circular dichroism spectroscopy, NMR, and crystallography, which are employed to investigate its secondary structure, conformational dynamics, and propensity for disorder or folding upon binding. Such studies provide detailed insights into the structural motifs that underpin Nup98's functional versatility, as well as the molecular determinants of its interactions with other NPC components or regulatory proteins.
Post-translational modification research: The peptide corresponding to residues 315-360 of Nup98 is also used as a substrate in enzymatic assays aimed at characterizing site-specific post-translational modifications, such as phosphorylation, sumoylation, or ubiquitination. By enabling precise mapping of modification sites and facilitating the study of their impact on Nup98's function, localization, or interaction profile, this peptide supports the elucidation of regulatory pathways governing nuclear pore complex dynamics and nucleoporin-mediated signaling events.
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