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93985

Adenosindeaminase human, rekombinant

Name: Adenosindeaminase human, rekombinant
Brand: SIGMA

recombinant, expressed in E. coli, ≥1 U/mL

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Über diesen Artikel

CAS-Nummer:

9026-93-1

UNSPSC Code:

12352204

EG-Nummer:

3.5.4.4 (BRENDA, IUBMB)

Specific activity:

≥1 U/mL

Recombinant:

expressed in E. coli

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Eigenschaften

recombinant

expressed in E. coli

form

liquid

specific activity

≥1 U/mL

storage temp.

−20°C

Beschreibung

Application

Adenosine deaminase (ADA) is a key enzyme in purine metabolism and is essential for normal immune function [1]. It is important in the study of immune system diseases such as rheumatoid arthritis [2]. 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 .

Other Notes

One unit will deaminate 1.0 μmole of adenosine to inosine per min at pH 7.5 at 25°C.

Lagerklasse

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Serum and synovial fluid adenosine deaminase activity in patients with rheumatoid arthritis, osteoarthritis, and reactive arthritis.

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

Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.

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

Cellular sensing of extracellular purine nucleosides triggers an innate IFN-β response.

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