Arylsulfatase E isoform 3 (503-517)

Arylsulfatase E isoform 3 (503-517) is a synthetic peptide fragment corresponding to amino acids 503 through 517 of the human Arylsulfatase E enzyme. As a defined peptide sequence, it represents a specific region within the Arylsulfatase E protein, which is a member of the sulfatase family involved in the hydrolysis of sulfate esters in biological systems. This peptide segment is of significant interest in biochemical research due to its relevance in protein structure-function analysis, post-translational modification studies, and antibody development. Its precise sequence allows for targeted investigations into the functional domains of Arylsulfatase E, supporting a range of applications in molecular biology, enzymology, and proteomics.

Epitope mapping: Researchers commonly utilize this peptide fragment in epitope mapping studies to identify antibody binding sites within Arylsulfatase E. By providing a defined segment of the protein, the peptide enables precise determination of immunogenic regions, facilitating the development and validation of specific antibodies for detection, quantification, or localization of the parent protein in complex biological samples.

Protein-protein interaction analysis: The 503-517 peptide serves as a valuable tool for dissecting protein-protein interactions involving Arylsulfatase E. By incorporating the peptide into binding assays, pull-down experiments, or surface plasmon resonance studies, scientists can characterize binding partners, map interaction domains, and elucidate molecular mechanisms underlying sulfatase-associated cellular pathways.

Post-translational modification studies: The defined sequence of this peptide allows for detailed investigation of potential post-translational modifications, such as phosphorylation or glycosylation, within the corresponding region of Arylsulfatase E. Synthetic peptides are especially useful for generating modified or labeled analogs, enabling the study of modification-specific effects on protein function, enzymatic activity, or cellular localization.

Peptide-based assay development: The fragment can be employed in the design and optimization of peptide-based assays that monitor enzymatic activity, substrate specificity, or inhibitor screening for Arylsulfatase E. Its use in enzyme-linked immunosorbent assays (ELISA), fluorescence polarization, or mass spectrometry-based workflows supports the quantitative and qualitative analysis of sulfatase-related biochemical processes.

Structural and functional analysis: Incorporating this peptide in structural studies, such as NMR spectroscopy or crystallography, provides insights into the conformational properties and functional motifs of Arylsulfatase E. By isolating a specific region of the protein, researchers can assess secondary structure, folding characteristics, or interactions with small molecules, contributing to a deeper understanding of the enzyme's biological role and regulatory mechanisms.

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