Anti-PARC CUL9 Antibody

The continued localization of p53 to the nucleus is essential for its function as a tumor suppressor. PARC, a large, Parkin-like ubiquitin ligase has recently been identified as a cytoplasmic anchor protein in p53-associated protein complexes. In the absence of stress, PARC inactivation results in nuclear localization of p53 and activation of p53-dependent apoptosis, while overexpression of this protein promoted cytoplasmic sequestration of p53. Surprisingly, PARC knockout mice were viable and exhibited no obvious phenotype, suggesting that other proteins, such as the highly related cullin family of E3 ubiquitin ligases, may perform similar functions in the absence of PARC. Additionally, it has been suggested that p53 binding to PARC may serve to control PARC function.

PARC antibody was raised against a 17 amino acid synthetic peptide from near the carboxy terminus of human PARC. The immunogen is located within the last 50 amino acids of PARC.

Core component of a Cul9-RING ubiquitin-protein ligase complex, a complex that mediates ubiquitination and subsequent degradation of BIRC5 and is required to maintain microtubule dynamics and genome integrity. Acts downstream of the 3M complex, which inhibits CUL9 activity, leading to prevent ubiquitination of BIRC5 (PubMed:24793696) . Cytoplasmic anchor protein in p53/TP53- associated protein complex. Regulates the subcellular localization of p53/TP53 and subsequent function (PubMed:12526791, PubMed:17332328) .

PARC antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.