Recombinant Human CANT1 Protein (His Tag) | PKSH030723

Recombinant Human CANT1 Protein (His Tag) | PKSH030723 | Gentaur US, UK & Europe Disrtribition

Synonyms: DBQD;SCAN-1;SCAN1;SHAPY

Active Protein: N/A

Activity: A DNA sequence encoding the human CANT1 (Q8WVQ1-1) extracellular domain (Gly 80-Ile 401) was fused with polyhistidine tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human CANT1 (Q8WVQ1-1) extracellular domain (Gly 80-Ile 401) was fused with polyhistidine tag at the N-terminus.

Fusion Tag: N-His

Species: Human

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 88 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 38 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: CANT1(calcium activated nucleotidase 1) belongs to the apyrase family. Apyrase is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP: ADP and another with no selectivity. It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate. CANT1 functions as a calcium-dependent nucleotidase with a preference for UDP. Defects in CANT1 are the cause of desbuquois dysplasia.

Research Area: N/A