93985
Adenosine deaminase human
recombinant, expressed in E. coli, ≥1 U/mL
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About This Item
Productos recomendados
recombinant
expressed in E. coli
form
liquid
specific activity
≥1 U/mL
storage temp.
−20°C
Application
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.
Biochem/physiol Actions
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 .
Unit Definition
One unit will deaminate 1.0 μmole of adenosine to inosine per min at pH 7.5 at 25°C.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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H Yuksel et al.
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
D K Wilson et al.
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
Rekha Dhanwani et al.
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
Yeon-Mi Lee et al.
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
George R Thompson et al.
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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