APC8 (D5O2D) Rabbit mAb #15100

Eukaryotic cell proliferation depends strictly upon the E3 ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C), whose main function is to trigger the transition of the cell cycle from metaphase to anaphase. The APC/C complex promotes the assembly of polyubiquitin chains on substrate proteins in order to target these proteins for degradation by the 26S proteasome (1,2). The vertebrate APC/C complex consists of as many as 15 subunits, including multiple scaffold proteins, two catalytic subunits (APC2, APC11), and a number of proteins responsible for substrate recognition (3). All E3 enzymes, including APC/C, utilize ubiquitin residues activated by E1 enzymes and transferred to E2 enzymes. Research studies indicate that APC/C interacts with the E2 enzymes UBE2S and UBE2C via the RING-finger domain-containing subunit APC11 (4-6). APC/C function relies on multiple cofactors, including an APC/C coactivator formed by the cell division control protein 20 homolog (CDC20) and Cdh1/FZR1. The CDC20/Cdh1 coactivator is responsible for recognition of APC/C substrates through interaction with specific D-box and KEN-box recognition elements within these substrates (7-9).
Anaphase-promoting complex subunit 8 (APC8, CDC23) is a component of the tetratricopeptide repeat (TPR) APC/C sub-complex that also includes APC3 (CDC27) and APC6 (CDC16). APC8 protein associates with APC3 and APC6 to facilitate recruitment of the APC/C coactivation subunits CDC20 and Cdh1/FZR1 (10,11). Research studies suggest that APC8 protein is overexpressed in papillary thyroid cancer and acts as an important regulator of cell cycle progression and cell growth (12).