CANT1 Protein, Human (HEK293, His)

N-His;Accession#Q8WVQ1-1 CANT1 (G80-I401)

CANT1, a calcium-dependent nucleotidase, exhibits a strong preference for UDP as its substrate, with the order of activity being UDP > GDP > UTP > GTP. Notably, it demonstrates very low activity towards ADP and even lower activity towards ATP, while it does not hydrolyze AMP and GMP. This enzymatic profile suggests a specific role in nucleotide metabolism. CANT1 is implicated in proteoglycan synthesis, indicating its involvement in processes related to the modification and regulation of these important macromolecules. The calcium-dependent nature of CANT1 highlights its regulation by intracellular calcium levels, adding an additional layer of complexity to its enzymatic function and potential cellular roles.

Measured by its ability to hydrolyze the beta 5'-phosphate group from the substrate uridine-5'-diphosphate (UDP) that incubate at room temperature for 20 min at 37°C. The orthophosphate product is measured by a Malachite Green Phosphate Detection Kit. The specific activity is 285089.234 pmol/min/μg.

Human

HEK293

N-6*His

Q8WVQ1-1 (G80-I401)

124583  [NCBI]

GQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI

Approximately 36-40 kDa due to the glycosylation.

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

Lyophilized powder

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<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.