- Peptide (C)GNLTKESPDTNGPK, corresponding to amino acid residues 1639-1652 of mouse AKAP12 (Accession Q9WTQ5). Intracellular, C-terminus.
- Western blot analysis of rat brain membranes (lanes 1 and 3) and mouse brain lysate (lanes 2 and 4):1,2. Anti-AKAP12 Antibody (#APZ-033), (1:200).
3,4. Anti-AKAP12 Antibody, preincubated with AKAP12 Blocking Peptide (#BLP-PZ033).
- Expression of AKAP12 in rat cerebellumImmunohistochemical staining of perfusion-fixed frozen rat brain sections with Anti-AKAP12 Antibody (#APZ-033), (1:400), followed by goat anti-rabbit-AlexaFluor-488. AKAP12 immunoreactivity (green) is detected in Purkinje cells and their dendritic trees (arrows). Cell nuclei are stained with DAPI (blue).
- Carnegie, G.K. et al. (2009) IUBMB Life 61, 394.
- Gelman, I.H. (2010) Genes Cancer 1, 1147.
- Han, B. et al. (2015) Pflugers Arch. 467, 2401.
- Langeberg, L.K. and Scott, J.D. (2005) J. Cell Sci. 118, 3217.
- Uhlén, M. et al. (2015) Science 347, 1260419.
- Wild, A.R. and Dell’Acqua, M.L. (2018) Pharmacol. Ther. 185, 99.
- Wong, W. and Scott, J.D. (2004) Nat. Rev. Mol. Cell. Biol. 5, 959.
- Wu, X. et al. (2018) Biomed. Environ. Sci. 31, 927.
The A-kinase anchoring protein 12 (AKAP12) belongs to a family of scaffold proteins, which anchor signaling proteins such as PKA in a spatiotemporal manner4. AKAPs generally bind PKA at their N-terminus, while the sequence at their C-terminus determines their spatial location4. To date, more than 50 AKAPs have been identified and perceived to integrate signaling pathways by anchoring multi-protein complexes1.
AKAP12 integrates diverse signaling pathways such as PKA, PKC, and β2-adrenergic receptor7,8. Similar to other members of this protein-family, AKAP12 contains a PKA binding domain. In addition, AKAP12 also contains a docking site for PKC2,6 and a myristoyl acid that sequesters it to the plasma membrane7.
AKAP12 is widely expressed in a variety of tissues with the highest expression in male and female reproductive organs, skeletal muscle, kidneys, and urinary tract5.
One of the most characterized activities of AKAP12 is regulation of the cell cycle3. AKAP12 controls two fundamental cell processes such as the G1/S transition and cytokinesis. In that being said, studies in NIH-3T3 fibroblasts, showed that ectopic expression of AKAP12 reduced cyclin D1 levels and the phosphorylation of its downstream target Rb, and consequently attenuated cell-cycle progression3. Furthermore, in HeLa cells, knockdown of AKAP12 resulted in profound changes in cell morphology, which indicates the inability of cells to divide3.
Given that AKAP12 plays a pivotal role in cell cycle regulation, it is not surprising that in some cases it is involved in cancer malignancies. It is now clear that AKAP12 is a key driver of gastrointestinal cancers such as colorectal cancer and hepatocellular carcinomas8.
Species reactivity key:
Anti-AKAP12 Antibody (#APZ-033) is a highly specific antibody directed against an epitope of the mouse protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize Gravin from mouse, rat, and human samples.