CECR1 Protein, Human (sf9, His)

CECR1, an adenosine deaminase, degrades extracellular adenosine, a pivotal signaling molecule, with activity dependent on elevated adenosine levels. It binds cell surfaces through proteoglycans, hinting at roles in cell proliferation and differentiation beyond its enzyme function. This dual functionality highlights its potential significance in cellular regulatory processes. CECR1 Protein, Human (sf9, His) is the recombinant human-derived CECR1 protein, expressed by Sf9 insect cells, with C-His labeled tag. The total length of CECR1 Protein, Human (sf9, His) is 511 a.a., with molecular weight of ~58 KDa.

CECR1, an adenosine deaminase, is implicated in the degradation of extracellular adenosine, a pivotal signaling molecule governing diverse cellular responses. Its enzymatic activity is contingent upon elevated adenosine levels. CECR1 exhibits a propensity to bind to cell surfaces through proteoglycans, suggesting a potential role in the modulation of cell proliferation and differentiation that extends beyond its canonical enzyme function. This dual functionality underscores its potential significance in intricate cellular regulatory processes.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

Sf9 insect cells

C-His

Q9NZK5 (M1-K511)

51816  [NCBI]

Approximately 58 kDa.

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, 10% Glycerol, pH 8.0. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.