Adenosine Deaminase (ADA)

Adenosine Deaminase (ADA) is present majorly in the proximal small intestine and the duodenum. It is also called Adenosine aminohydrolase. It is a zinc metalloenzyme and exists as a high (230−440 kDa) and low molecular weight (30−47 kDa) isoforms.

Adenosine deaminase (ADA) is a zinc metalloenzyme.

Adenosine Deaminase (ADA) has been used as a component of macrophage- serum-free media (SFM) to treat macrophages.

Adenosine deaminase has been used to pre-treat primary Kupffer cells.

Adenosine Deaminase (ADA) catalyzes the deamination of adenosine analogs to the corresponding inosine analogs. It is present in high levels in colorectal cancer and is a potential marker in tuberculous pleuriti. ADA deficiency affects T-and B-lymphocytes resulting in severe combined immunodeficiency (SCID) leading to lymphocytopenia.

Adenosine deaminase (ADA) is involved in the deamination of adenosine to inosine and 2′ deoxyadenosine to 2′-deoxyinosine.

Solution in 50% glycerol (v/v), 10 mM potassium phosphate, pH approximately 6

Storage conditions (working solution): ADA (all preparations) may be dialyzed, without loss of activity, at 2 to 8 °C against 20 mM phosphate buffer, pH 7. The dialyzed preparation is stable at -15 to -25 °C.

Contaminants: <0.01% alkaline phosphatase, AMP-deaminase, guanase, and nucleoside phosphorylase each

For life science research only. Not for use in diagnostic procedures.