Recombinant Human CANT1 protein (His tag N-Terminus)
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Recombinant Human CANT1 protein (His tag N-Terminus) is a Human Fragment protein, in the 63 to 401 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
SHAPY, CANT1, Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human CANT1 protein (His tag N-Terminus) (AB123189)
15% SDS-PAGE showing ab123189 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CANT1 influences cellular processes by regulating extracellular nucleotide signaling. It involves in protein glycosylation a process critical for protein folding and stability. CANT1 does not form part of a complex but functions independently to exert its biological effects. Glycosylation impacts how proteins function and signal across the body reflecting the importance of CANT1's enzymatic role in various cells.
Pathways
Multiple cellular pathways depend on CANT1’s enzymatic activity. The protein is notably engaged in the purinergic signaling pathway where it modulates extracellular nucleotide levels that influence signaling cascades. CANT1 shares functional relationships with proteins such as ENTPD5 and NTPDases which partake in similar nucleotide hydrolysis processes. It also has connections to metabolic processes within glucose metabolism.
Specifications
Form
Liquid
Additional notes
ab123189 is purified using conventional chromatography techniques.
General info
Function
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP (PubMed : 12234496, PubMed : 15006348, PubMed : 15248776, PubMed : 16835225). Involved in proteoglycan synthesis (PubMed : 22539336).
Sequence similarities
Belongs to the apyrase family.
Post-translational modifications
N-glycosylated.
Target data
Complementary Products
Product promise
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