APC10 Antibody

Product Usage Information

Storage

Specificity / Sensitivity

Species Reactivity:

Human, Mouse, Rat, Monkey

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human APC10 protein. Antibodies are purified by protein A and peptide affinity chromatography.

Background

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 10 (APC10, DOC1) is a highly conserved, core component of the anaphase promoting complex/cyclosome (10,11). Research studies indicate that APC10 participates in substrate recognition by the APC/C (3,12,13).