Anti-Tankyrase-2 Antibody, clone 2F5.1 clone 2F5.1, from mouse

Tankyrase-2 (EC 2.4.2.30; UniProt Q9H2K2; also known as ADP-ribosyltransferase diphtheria toxin-like 6, ARTD6, PARP-5B, Poly [ADP-ribose] polymerase 5B, TANK2, TNKS-2, Tankyrase II, Tankyrase-like protein, Tankyrase-related protein, TRF1-interacting ankyrin-related ADP-ribose polymerase 2) is encoded by the TNKS2 (also known as PARP5B, TANK2, TNKL) gene (Gene ID 80351) in human. Tankyrase-2 belongs to the poly(ADP-ribosylation) polymerase (PARP) family of enzymes that mediate post-translational modification of proteins by poly(ADP-ribosyl)ation, where repeating units of ADP-ribose linked by glycosidic bonds were added to aspartate, glutamate, asparagine, arginine or lysine residues of substrate proteins. Poly(ADP-ribose) (PAR) modification is reversible through the action of poly(ADP-ribose) glycohydrolase (PARG) and ADP-ribosyl protein lyase. Tankyrase-2 and the related Tankyrase-1 share a common domain organization with 15 N-terminal ankyrin-repeats (a.a. 57-776 in TNKS2) involved in substrate recognition, a sterile alpha motif (SAM) domain (a.a. 873-936 in TNKS2) required for dimerization, followed by the C-terminal PARP domain (a.a. 959-1164 in TNKS2). Mice with either Tnks1- or Tnks2-knockout are viable, while double Tnks1-/Tnks2-knockout is lethal at embryonic day 9.5, suggesting a functional redundancy between these two enzymes. Both tankyrases target and suppress Axin2, a well known beta-catenin negative regulator. Tankyrase-2 ribosylates Src-binding adapter protein 3BP2, leading to its ubiquitination and proteasomal degradation in macrophages and osteoclasts. Loss of tankyrase-mediated 3BP2 negative regulation underlies the pathogenic mechanism of cherubism, an autosomal dominant disorder affecting cranial bone development.