93985
Adenosine deaminase human
recombinant, expressed in E. coli, ≥1 U/mL
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About This Item
Prodotti consigliati
Ricombinante
expressed in E. coli
Forma fisica
liquid
Attività specifica
≥1 U/mL
Temperatura di conservazione
−20°C
Applicazioni
Adenosine deaminase (ADA) is a key enzyme in purine metabolism and is essential for normal immune function . It is important in the study of immune system diseases such as rheumatoid arthritis . Product 93985 is from human, is recombinant and is expressed in E. coli.
Azioni biochim/fisiol
Adenosine deaminase irreversibly deaminates adenosine to inosine. In addition to immune system regulation, ADA may be involved in epithelial cell differentiation, neurotransmission and gestation maintenance .
Definizione di unità
One unit will deaminate 1.0 μmole of adenosine to inosine per min at pH 7.5 at 25°C.
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Certificati d'analisi (COA)
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Annals of the rheumatic diseases, 47(6), 492-495 (1988-06-01)
Adenosine deaminase activity was determined in paired samples of serum and synovial fluid taken from patients with rheumatoid arthritis (n = 12), reactive arthritis (n = 13), and osteoarthritis (n = 7), and the value of this investigation in the
Science (New York, N.Y.), 252(5010), 1278-1284 (1991-05-31)
The crystal structure of a murine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, has been determined and refined at 2.4 angstrom resolution. The structure is folded as an eight-stranded parallel alpha/beta barrel with a deep pocket
Science advances, 6(30), eaba3688-eaba3688 (2020-08-04)
Mechanisms linking immune sensing of DNA danger signals in the extracellular environment to innate pathways in the cytosol are poorly understood. Here, we identify a previously unidentified immune-metabolic axis by which cells respond to purine nucleosides and trigger a type
Biophysical chemistry, 172, 18-25 (2013-01-22)
Human ADAR1, which has two left-handed Z-DNA binding domains, preferentially binds Z-DNA rather than B-DNA with a high binding affinity. Z-DNA can be induced in long genomic DNA by Z-DNA binding proteins through the formation of two B-Z junctions with
Chest, 143(3), 776-781 (2012-11-29)
In a patient with positive serum serology for coccidioidomycosis, the differential diagnosis of concurrent pleural effusions can be challenging. We, therefore, sought to clarify the performance characteristics of biochemical, serologic, and nucleic-acid-based testing in an attempt to avoid invasive procedures.
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