HERPUD1 Antibody / Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, 100 ug

HERPUD1 antibody detects Homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 1, encoded by the HERPUD1 gene on chromosome 16q13. HERPUD1 antibody is commonly used to study this endoplasmic reticulum (ER)-resident protein that participates in protein quality control, ER stress responses, and the unfolded protein response (UPR). HERPUD1 is highly induced by ER stress conditions such as hypoxia, oxidative damage, or accumulation of misfolded proteins. Its protective function lies in facilitating ER-associated degradation (ERAD), a pathway that retrotranslocates misfolded proteins from the ER to the cytosol for ubiquitin-proteasome degradation.

Structurally, HERPUD1 contains a ubiquitin-like (UBL) domain that mediates interaction with proteasome subunits and ubiquitin-conjugating enzymes. Its N-terminal transmembrane region anchors it to the ER membrane, while its cytoplasmic tail recruits E3 ligases and cofactors. These features allow HERPUD1 to function as a scaffold for protein degradation complexes, ensuring efficient clearance of unfolded proteins. Its rapid upregulation during ER stress highlights its role as a first responder in the UPR.

Functionally, HERPUD1 protects cells from ER stress-induced apoptosis. By promoting protein degradation, it prevents accumulation of misfolded proteins and maintains ER homeostasis. Beyond ERAD, HERPUD1 influences calcium homeostasis and autophagy. Knockout studies demonstrate increased susceptibility to ER stress and impaired survival under hypoxia. Researchers use HERPUD1 antibody to study UPR signaling, proteostasis, and mechanisms of cell survival under stress.

Clinically, HERPUD1 has been implicated in neurodegenerative disorders such as Parkinson's disease and Alzheimer's disease, where chronic ER stress contributes to neuronal death. In cancer, HERPUD1 expression correlates with tumor survival in hypoxic environments, suggesting it may support tumor adaptation to stress. Polymorphisms in HERPUD1 have been linked to cardiovascular disease risk, reflecting its role in stress adaptation. Elevated expression has also been observed in kidney disease and diabetes, where ER stress drives pathology.

Experimentally, HERPUD1 antibody is applied in western blotting to detect the ~54 kDa protein, in immunofluorescence microscopy to study ER localization, and in immunohistochemistry to assess expression in tissues under stress. Co-immunoprecipitation with HERPUD1 antibody has identified its interactions with ubiquitin ligases, proteasomal components, and ER chaperones. NSJ Bioreagents provides HERPUD1 antibody to support research in ER stress, neurodegeneration, oncology, and cardiovascular biology.