Anti-ADA Antibody Picoband® Fluoro647 Conjugated

Adenosine Deaminase (also known as adenosine aminohydrolase, or ADA) is an enzyme involved in purine metabolism. Primarily, ADA in humans is involved in the development and maintenance of the immune system. However, ADA association has also been observed with epithelial cell differentiation, neurotransmission, and gestation maintenance. It has also been proposed that ADA, in addition to adenosine breakdown, stimulates release of excitatory amino acids and is necessary to the coupling of A1 adenosine receptors and heterotrimeric G proteins. Adenosine deaminase deficiency leads to pulmonary fibrosis, suggesting that chronic exposure to high levels of adenosine can exacerbate inflammation responses rather than suppressing them. It has also been recognized that adenosine deaminase protein and activity is upregulated in mouse hearts that overexpress HIF-1 alpha, which in part explains the attenuated levels of adenosine in HIF-1 alpha expressing hearts during ischemic stress.

E. coli-derived human ADA recombinant protein (Position: Q135-L363) . Human ADA shares 82.5% and 82.9% amino acid (aa) sequence identity with mouse and rat ADA, respectively.

Cancer, Cancer Metabolism, Chromatin Modifying Enzymes, Epigenetics and Nuclear Signaling, Metabolism, Metabolism Processes, Pathways and Processes, Response To Hypoxia

Catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes inly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte- epithelial cell adhesion. .

1. Blackburn MR (2003) . Too much of a good thing: adenosine overload in adenosine-deaminase-deficient mice. Trends in Pharmacological Sciences 24 (2) : 66–70. 2. Cristalli G, Costanzi S, Lambertucci C, Lupidi G, Vittori S, Volpini R, Camaioni E (Mar 2001) . Adenosine deaminase: functional implications and different classes of inhibitors. Medicinal Research Reviews 21 (2) : 105–128. 3. Wilson DK, Rudolph FB, Quiocho FA (May 1991) . Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science 252 (5010) : 1278–1284.

Cell membrane; Peripheral membrane protein; Extracellular side. Cell junction. Cytoplasmic vesicle lumen . Cytoplasm . Colocalized with DPP4 at the cell junction in lymphocyte-epithelial cell adhesion.