Anti-ARF-BP1 HUWE1 Antibody

The ARF tumor suppressor is a critical regulator of p53 stability. In addition to p53, ARF1 binds to other proteins such as MDM2 and ARF-BP1, a large protein containing HECT, UBA and WWE motifs. ARF-BP1 directly binds and ubiquitinates p53; this activity is inhibited by ARF, indicating that ARF-BP1 is a critical mediator of the p53-dependent and p53-independent tumor suppressor functions of ARF. ARF-BP1 can also catalyze the polyubiquitination of Mcl-1, an anti-apoptotic Bcl-2 family member involved in DNA damage-induced apoptosis. Elimination of ARF-BP1 expression by RNA interference stabilized Mcl-1 protein, resulting in an attenuation of apoptosis induced by DNA-damage agents.

ARF-BP1 antibody was raised against a 19 amino acid synthetic peptide from near the carboxy terminus of human ARF-BP1. The immunogen is located within amino acids 4250 - 4300 of ARF-BP1.

Weakly expressed in heart, brain and placenta but not in other tissues. Expressed in a number of cell lines, predominantly in those from colorectal carcinomas.

E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Binds to an upstream initiator-like sequence in the preprodynorphin gene. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation. Mediates polyubiquitination of isoform 2 of PA2G4.