SPCS2 (Signal Peptidase Complex Subunit 2) is a key component of the endoplasmic reticulum (ER)-resident signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal peptides from nascent secretory and membrane proteins during their translocation into the ER. As part of the SPC, SPCS2 plays a critical role in protein maturation, trafficking, and quality control. Dysregulation of SPCS2 has been implicated in various diseases, including viral infections (e.g., flaviviruses exploit the SPC for viral polyprotein processing) and neurodegenerative disorders linked to ER stress.
Antibodies targeting SPCS2 are essential tools for studying its expression, localization, and function in cellular models. They are widely used in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to investigate SPC assembly, ER-associated degradation (ERAD), and cellular responses to secretory pathway stress. SPCS2-specific antibodies also aid in exploring its interaction with viral proteins or disease-associated mutants.
Recent studies highlight SPCS2's potential as a therapeutic target, particularly in antiviral strategies or conditions involving proteostasis imbalance. Validated SPCS2 antibodies (e.g., from commercial sources like Abcam or Sigma-Aldrich) often undergo rigorous specificity testing, including knockout cell line validation, ensuring reliability in both basic research and translational applications.