Anti-CUL2 (C-terminal) polyclonal antibody

A tridentate hydrazone precursor, N'-[1-(pyridin-2-yl)ethylidene]acetohydrazide (L) (1:1 refluxed product of acetichydrazide and 2-acetylpyridine), produced two octahedral Cu-II and Ni-II derivatives, [CuL2]center dot NO3 (1) and [NiL2]center dot ClO4 center dot H2O (2). Both are subjected to X-ray diffraction system, and structural investigation shows that the central metal atom (Cu-II or Ni-II) adopts a distorted octahedral geometry with N4O2 donor sets by coordination of a pair of independent hydrazone precursors. Besides X-ray study, IR and UV-vis spectra, thermal analysis and room temperature magnetic moments are utilized for establishing significant characteristics of both complexes. It is apparent that the M-N-pyridine bonds are slightly longer than the M-N-imino bonds, Cu1-N1 and Cu1-N4 [2.300(2) and 2.038(2) ] for 1 and Ni1-N1 and Ni1-N4 [2.075(2) and 2.084(1) ] for 2, Cu1-N2 and Cu1-N5 [2.062(1) and 1.932(1) ] for 1 and Ni1-N2 and Ni1-N5 [2.008(2) and 1.975(2) ] for 2, respectively. As per our observation, the effective magnetic moment value (A mu(eff)) is found to be 1.77 B.M. for 1 and 3.06 BM for 2, respectively.

Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1.