Adenosine Deaminase/ADA Protein, Human (sf9, His)

The adenosine deaminase/ADA protein catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine, which is critical for purine metabolism and adenosine homeostasis. It affects cell signaling indirectly by regulating extracellular adenosine. Adenosine Deaminase/ADA Protein, Human (sf9, His) is the recombinant human-derived Adenosine Deaminase/ADA protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of Adenosine Deaminase/ADA Protein, Human (sf9, His) is 363 a.a., with molecular weight of ~44 kDa.

Adenosine Deaminase (ADA) protein serves as a crucial enzyme, orchestrating the hydrolytic deamination of adenosine and 2-deoxyadenosine. This enzymatic activity is fundamental to purine metabolism and contributes significantly to adenosine homeostasis. Beyond its direct role in nucleotide catabolism, ADA plays a multifaceted role in cellular signaling events. It acts as a positive regulator of T-cell coactivation, influencing lymphocyte-epithelial cell adhesion through its interaction with DPP4. Additionally, ADA enhances dendritic cell immunogenicity, affecting costimulatory molecule expression and cytokine secretion. The protein also modulates adenosine receptors ADORA1 and ADORA2A, contributing to ligand affinity via conformational changes. Furthermore, ADA participates in plasminogen activation, influences CD4+ T-cell differentiation and proliferation, and plays roles in male fertility and early postimplantation embryonic development.

Human

Sf9 insect cells

C-His

P00813 (M1-L363)

100  [NCBI]

Approximately 44 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.