Recombinant Human ENPP1/PC1 protein
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(1 Publication)
Recombinant Human ENPP1/PC1 protein is a Human Fragment protein, in the 98 to 925 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
M6S1, NPPS, PC1, PDNP1, ENPP1, Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Alkaline phosphodiesterase I, Membrane component chromosome 6 surface marker 1, Nucleotide diphosphatase, Nucleotide pyrophosphatase, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, NPPase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human ENPP1/PC1 protein (AB167943)
10% SDS-PAGE analysis of ab167943.
Lane 1 : reduced and boiled sample, 2.5μg/lane.
Lane 2 : non-reduced and non-boiled sample, 2.5μg/lane.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ENPP1 significantly influences bone mineralization and soft tissue calcification. It interacts with proteins like ectonucleoside triphosphate diphosphohydrolase-1 (ENTPD1) impacting cellular uptake of calcified materials. The protein is also involved in the regulatory networks responsible for controlling insulin signaling impacting metabolic processes. ENPP1 may form complexes with other proteins which can finely tune its biological activity and effects.
Pathways
ENPP1 plays a role in the insulin signaling pathway and the pyrophosphate pathway. Via its participation in insulin signaling ENPP1 regulates glucose metabolism and influences insulin sensitivity. It affects pathways related to mineral metabolism where it interacts with proteins like ENPP3. By regulating extracellular pyrophosphate levels ENPP1 contributes to inorganic phosphate homeostasis and influences skeletal development and maintenance.
Specifications
Form
Lyophilized
Additional notes
ab167943 was purifed using Ni-NTA chromatography.
General info
Function
Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (By similarity). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed : 11004006). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed : 25344812, PubMed : 27467858, PubMed : 28011303, PubMed : 35147247, PubMed : 8001561). May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed : 27467858, PubMed : 8001561). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (By similarity). Appears to modulate insulin sensitivity and function (PubMed : 10615944). Also involved in melanogenesis (PubMed : 28964717). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed : 25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (PubMed : 25344812). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3'-3'-cGAMP (PubMed : 25344812).
Sequence similarities
Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.
Post-translational modifications
Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.. N-glycosylated.. The secreted form is produced through cleavage at Lys-103 by intracellular processing.
Target data
Publications (1)
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BioMed research international 2019:5214821 PubMed30800670
2019
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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