SPOP antibodies target the 42 kDa nuclear protein containing MATH and BTB/POZ domains, which mediates substrate recruitment for CUL3-dependent ubiquitination . Key applications include:
Prostate Cancer: SPOP mutations (e.g., F133V) disrupt substrate binding, stabilizing oncoproteins like AR and ERG . Wild-type SPOP suppresses tumor growth by degrading PD-L1 and TRIM24 .
Renal Cell Carcinoma: Cytoplasmic SPOP accumulation correlates with increased proliferation markers (PCNA, p-Histone H3) and phosphorylated Bax, promoting anti-apoptotic effects .
Hepatocellular Carcinoma: SPOP ubiquitinates IRF2BP2, attenuating its tumor-suppressive effects on cell migration .
SPOP degrades MyD88 via K48-linked ubiquitination, limiting NF-κB activation and IL-1β production during Salmonella infection .
In IFNγ-stimulated cells, SPOP depletion elevates IRF1 levels, enhancing antiviral responses against VSV .
Dilution Ranges:
Controls: Use SPOP knockout cell lines (e.g., ab277845) to confirm signal specificity .
Storage: Stable for 1 year at 2–8°C (Sigma) or -20°C long-term (Proteintech) .
Substrate Diversity: SPOP interacts with >50 substrates, including transcription factors (GLI2, c-MYC), DNA repair proteins (BRMS1), and immune regulators (IRF1) .
Therapeutic Implications: SPOP loss sensitizes cancer cells to DNA-damaging agents (e.g., camptothecin) , while its overexpression reverses chemotherapy resistance in leukemia .