Anti-VPAC2/VIPR2 Antibody Picoband®

Vasoactive intestinal peptide receptor 2 also known as VPAC2, is a G-protein coupled receptor that in humans is encoded by the VIPR2 gene. This gene encodes a receptor for vasoactive intestinal peptide, a small neuropeptide. Vasoactive intestinal peptide is involved in smooth muscle relaxation, exocrine and endocrine secretion, and water and ion flux in lung and intestinal epithelia. Its actions are effected through integral membrane receptors associated with a guanine nucleotide binding protein which activates adenylate cyclase.

NAD-dependent protein lipoamidase sirtuin-4, mitochondrial; NAD-dependent ADP-ribosyltransferase sirtuin-4; NAD-dependent protein deacetylase sirtuin-4; Regulatory protein SIR2 homolog 4; SIR2-like protein 4; SIRT4; SIR2L4

A synthetic peptide corresponding to a sequence at the N-terminus of human VPAC2/VIPR2, which shares 94.4% and 85% amino acid (aa) sequence identity with mouse and rat VIPR2, respectively.

Detected in vascular smooth muscle and striated muscle. Detected in insulin-producing beta-cells in pancreas islets of Langerhans (at protein level) . Widely expressed. Weakly expressed in leukocytes and fetal thymus.

Acetylation, Atherosclerosis, Cancer, Cardiovascular, Cell Biology, Chromatin Modifying Enzymes, Diabetes, Diabetes-associated, Energy Metabolism, Energy Transfer Pathways, Epigenetics and Nuclear Signaling, Heart Disease, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction

Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA interaction probably through the regulation of NAD+ levels. Down-regulates insulin secretion.

1. Adamou, J. E., Aiyar, N., Van Horn, S., Elshourbagy, N. A. Cloning and functional characterization of the human vasoactive intestinal peptide (VIP) -2 receptor. Biochem. Biophys. Res. Commun. 209: 385-392, 1995. 2. Harmar, A. J., Marston, H. M., Shen, S., Spratt, C., West, K. M., Sheward, W. J., Morrison, C. F., Dorin, J. R., Piggins, H. D., Reubi, J.-C., Kelly, J. S., Maywood, E. S., Hastings, M. H. The VPAC2 receptor is essential for circadian function in the mouse suprachiasmatic nuclei. Cell 109: 497-508, 2002. 3. Mackay, M., Fantes, J., Scherer, S., Boyle, S., West, K., Tsui, L.-C., Belloni, E., Lutz, E., Van Heyningen, V., Harmar, A. J. Chromosomal localization in mouse and human of the vasoactive intestinal peptide receptor type 2 gene: a possible contributor to the holoprosencephaly 3 phenotype. Genomics 37: 345-353, 1996.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.