CANT1 Protein, Human (HEK293, Fc)

CANT1 is a calcium-dependent nucleotidase that shows a clear preference for UDP, and the order of its enzymatic activity is UDP > GDP > UTP > GTP. It is worth noting that it has little activity on ADP and even less activity on ATP, but it does not hydrolyze AMP and GMP. CANT1 Protein, Human (HEK293, Fc) is the recombinant human-derived CANT1 protein, expressed by HEK293 , with N-hFc labeled tag.

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.

Human

HEK293

N-hFc

Q8WVQ1-1 (G80-I401)

124583  [NCBI]

Partial

GQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI

Approximately 65 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.