Human ISOC2 and Recombinant ISOC2 Proteins in Molecular and Biochemical Research

Isochorismatase domain-containing proteins constitute a conserved class of enzymes found across multiple biological kingdoms. In humans, the ISOC2 gene (Isochorismatase Domain Containing 2) encodes a protein that has attracted attention due to its structural conservation, intracellular localisation, and documented protein–protein interactions. Although its precise physiological substrate has not yet been conclusively identified, ISOC2 continues to be investigated as part of broader efforts to understand intracellular regulation, protein stability, and cell-cycle associated pathways.

This article provides a technical overview of ISOC2 biology, focusing on its genomic annotation, structural features, experimental relevance, and the use of recombinant ISOC2 proteins as laboratory reagents. All statements are grounded in publicly available academic and government-hosted sources, making the discussion suitable for expert researchers and advanced laboratories.

The ISOC2 gene is a protein-coding locus curated by the U.S. National Center for Biotechnology Information (NCBI). It is annotated within the human genome and catalogued with stable identifiers that facilitate cross-database integration across genomics and proteomics platforms.

Authoritative genomic information is available through the NCBI Gene database

This resource provides detailed information on gene location, exon structure, curated references, and cross-links to protein and transcript records. Additional annotation is supplied by the Alliance of Genome Resources, which integrates data from multiple NIH-funded and academic consortia

Together, these databases establish ISOC2 as a conserved human gene with experimentally validated expression and molecular relevance.

The ISOC2 protein contains a conserved isochorismatase-like domain, a fold historically associated with enzymatic hydrolysis reactions in microbial and eukaryotic systems. Structural classification and sequence curation are provided by UniProt, a joint initiative involving EMBL-EBI and academic partners:

Isochorismatase domains are discussed in protein family databases and structural biology references maintained by academic institutions, including:

https://scop.berkeley.edu/

While the enzymatic activity of human ISOC2 remains under investigation, conservation of the fold suggests functional relevance that justifies continued biochemical study.

Experimental and curated data indicate that ISOC2 localises to multiple intracellular compartments, including the cytoplasm, nucleus, and mitochondria. Such distribution patterns are consistent with proteins involved in regulatory and interaction-based functions rather than highly compartmentalised metabolic enzymes.

Evidence for protein–protein interaction has been documented in peer-reviewed literature indexed by PubMed (U.S. National Library of Medicine):

This study describes an interaction between ISOC2 and the cyclin-dependent kinase inhibitor p16^INK4a, a central regulator of cell-cycle progression. Supporting interaction data are also aggregated in academic repositories such as BioGRID

These findings support the hypothesis that ISOC2 may participate in regulatory protein networks rather than acting solely as a metabolic enzyme.

Functional annotations associated with ISOC2 include protein binding and intracellular localisation terms, curated through Gene Ontology (GO) frameworks supported by NIH and university consortia:

Although no definitive disease associations have been established in clinical databases such as OMIM or ClinVar, ISOC2 continues to be explored within broader studies of cellular regulation, protein stability, and molecular ageing mechanisms.

Background on experimental strategies used to investigate such proteins can be found in NIH-hosted educational resources, including:

https://www.ncbi.nlm.nih.gov/books/NBK26828/

These materials provide methodological context for researchers employing recombinant proteins in functional assays.

Recombinant human proteins are essential tools in modern molecular biology, enabling controlled studies of protein structure, interaction dynamics, and biochemical behaviour. Recombinant ISOC2 proteins are commonly employed in in vitro binding assays, antibody validation, and structural investigations where endogenous expression levels may be insufficient or experimentally impractical.

Such reagents are typically produced using bacterial expression systems and purified under conditions compatible with downstream biochemical applications. Detailed guidance on recombinant protein expression and purification is available from university and government educational sources, including:

https://pmc.ncbi.nlm.nih.gov/articles/PMC7148393/

For laboratories seeking access to recombinant ISOC2 proteins, specialist research suppliers make these reagents available for non-clinical use. GenPrice offers recombinant ISOC2 as part of its research-grade protein catalogue, allowing investigators to source the protein for experimental workflows without the need for in-house expression and purification.

Researchers may shop through GenPrice or review available ISOC2 offerings to determine suitability for their specific experimental designs.

ISOC2 represents a class of human proteins that are structurally conserved yet functionally underexplored. Its documented interaction with cell-cycle regulatory proteins, combined with its conserved domain architecture, makes it a subject of interest in fundamental research rather than applied or clinical contexts.

Publicly funded databases and academic resources continue to play a critical role in shaping our understanding of ISOC2. Key reference platforms include:

https://pubmed.ncbi.nlm.nih.gov/

https://www.ncbi.nlm.nih.gov/gene/

https://www.uniprot.org/

Continued investigation using recombinant protein reagents will be essential for elucidating the molecular role of ISOC2 in human cells.

This article is intended for research and educational purposes only and reflects current publicly available knowledge. Recombinant ISOC2 proteins discussed herein are for laboratory research use and not intended for diagnostic or therapeutic applications.