HERC4 Antibody / HECT domain and RCC1-like domain-containing protein 4, 100 ug

HERC4 antibody detects Probable E3 ubiquitin-protein ligase HERC4, a member of the HERC family of ubiquitin ligases that mediate selective protein ubiquitination and degradation. Encoded by the HERC4 gene on chromosome 10q22.1, this large enzyme (approximately 1100 amino acids) contains an N-terminal RCC1-like domain and a C-terminal HECT domain that catalyzes the transfer of ubiquitin from E2 conjugating enzymes to target substrates. Through this mechanism, HERC4 regulates diverse cellular processes including DNA repair, mitochondrial quality control, and spermatogenesis. As a multifunctional E3 ligase, it controls protein turnover and signaling by directing specific substrates to the proteasome for degradation.

HERC4 expression is widespread but most pronounced in testis, brain, and skeletal muscle. Functional studies have demonstrated roles in germ cell differentiation and embryonic development. In the testis, HERC4 localizes to elongating spermatids and regulates ubiquitin-dependent remodeling of proteins essential for sperm maturation. Loss of HERC4 in model organisms leads to male infertility and abnormal spermatid morphology, confirming its requirement for spermatogenesis. In somatic tissues, HERC4 participates in protein quality control and signaling regulation, including modulation of TGF-beta and Wnt pathways.

The HERC4 antibody is commonly used in cell biology and reproductive biology research to detect HERC4 protein expression and localization. Western blot analysis typically reveals a 120 kilodalton band corresponding to the ligase, while immunofluorescence shows cytoplasmic and perinuclear localization consistent with its role in ubiquitin-mediated trafficking. Elevated HERC4 expression has been reported in several cancer types, including breast and liver carcinoma, where it promotes degradation of tumor suppressors and supports proliferation. Because HERC4 also influences mitochondrial dynamics, the antibody is valuable for studies examining proteostasis, signaling, and metabolism.

Mechanistically, HERC4 acts through its HECT domain to catalyze the formation of polyubiquitin chains, often targeting regulatory proteins involved in stress response and apoptosis. It interacts with molecular chaperones and ubiquitin ligase adaptors to fine-tune degradation specificity. Dysregulation of HERC4 activity leads to aberrant protein accumulation and altered signaling balance. The HERC4 antibody is therefore a versatile tool for exploring E3 ligase function in development, reproduction, and cancer biology. NSJ Bioreagents provides this antibody validated for its applications, ensuring specificity for HERC4 across human and model systems.