NASP antibody / Nuclear autoantigenic sperm, 100 ug

NASP antibody detects Nuclear autoantigenic sperm protein, encoded by the NASP gene on chromosome 1q24.2. NASP antibody is widely used in studies of histone metabolism, chromatin biology, and fertility. NASP is a histone chaperone that binds histones H1 and H3/H4, facilitating their storage, transport, and deposition onto DNA during chromatin assembly. By regulating histone availability, NASP ensures proper nucleosome formation, DNA replication, and cell cycle progression.

Structurally, NASP is a ~85 kDa protein that exists in two major isoforms: somatic NASP and testis-specific NASP. Both isoforms contain tetratricopeptide repeat (TPR) domains that mediate histone binding and interactions with other chaperones. Testis-specific NASP is highly expressed in germ cells and plays essential roles in spermatogenesis. Somatic NASP is expressed broadly across proliferating cells, including embryonic and cancer cells.

Functionally, NASP delivers histones to chromatin assembly factors and prevents their aggregation or degradation. It partners with histone-binding proteins such as ASF1 and HSPA2 to facilitate nucleosome assembly. By regulating histone pools, NASP maintains genomic stability and supports DNA replication. Researchers use NASP antibody to investigate chromatin assembly, fertility, and cancer biology.

Clinically, NASP is implicated in infertility, particularly male infertility, due to its essential role in spermatogenesis. Dysregulation of NASP has also been reported in cancers, where altered histone chaperone function contributes to genomic instability and abnormal gene expression. Autoantibodies against NASP have been described in certain autoimmune conditions. NSJ Bioreagents supplies NASP antibody for research in fertility, chromatin regulation, and oncology.

Experimentally, NASP antibody is used in western blotting to detect both somatic and testis-specific isoforms, in immunohistochemistry to analyze germ cell and tumor tissue expression, and in co-immunoprecipitation to study histone-chaperone complexes.