Biotinylated Human ENPP-3 (48-157) Protein 3369

$525.00 – $1,750.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Leu48-Asp157

available size

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SKU: 3369parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	N-His-Avi
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Ectonucleotide pyrophosphatase-phosphodiesterase 3 (ENPP3), a protein detected in the human uterus, has been found to play an important role in the development and invasion of tumours. It was recently discovered that ENPP3 was upregulated during the window of implantation in the human endometrium but its functional relevance remains elusive.
molecular weight	The protein has a predicted MW of 17.21 kDa. Due to glycosylation, the protein migrates to 18-20 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per ug by the LAL method.

Biotinylated Human ENPP-3 (48-157) Protein 3369

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Ectonucleotide pyrophosphatase-phosphodiesterase 3 (ENPP3), a protein detected in the human uterus, has been found to play an important role in the development and invasion of tumours. It was recently discovered that ENPP3 was upregulated during the window of implantation in the human endometrium but its functional relevance remains elusive.
Protein names Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (NPP3) (Alkaline phosphodiesterase I) (EC 3.1.4.1) (Dinucleoside polyphosphatase) (EC 3.6.1.-) (Nucleotide diphosphatase) (Nucleotide pyrophosphatase) (NPPase) (EC 3.6.1.9) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (CD antigen CD203c)
Gene names ENPP3,ENPP3 PDNP3
Protein family Nucleotide pyrophosphatase/phosphodiesterase family
Mass 100124Da
Function FUNCTION: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (PubMed:29717535, PubMed:9344668). Limits mast cells and basophils response during inflammation and during the chronic phases of allergic responses by eliminating extracellular ATP, a signaling molecule activating these cells in an autocrine manner. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (By similarity). Has a broad specificity and can also hydrolyze UDP-GlcNAc into UMP and GlcNAc-1-phosphate and potentially several other intracellular nucleotide sugars, including UDP-GalNAc, CMP-NeuAc, GDP-Fuc, and UDP-GlcA. Thereby, could modulate glycan biosynthesis and protein glycosylation (By similarity). Can hydrolyze extracellular dinucleoside polyphosphates, including the vasoactive adenosine polyphosphates as well (PubMed:12846830). In addition, displays an alkaline phosphodiesterase activity in vitro (PubMed:11342463). {ECO:0000250\|UniProtKB:Q6DYE8, ECO:0000269\|PubMed:11342463, ECO:0000269\|PubMed:12846830, ECO:0000269\|PubMed:29717535, ECO:0000269\|PubMed:9344668}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9; Evidence={ECO:0000269\|PubMed:29717535}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23997; Evidence={ECO:0000305\|PubMed:29717535}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = AMP + diphosphate + H(+); Xref=Rhea:RHEA:14245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:456215; EC=3.6.1.9; Evidence={ECO:0000269\|PubMed:29717535}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14246; Evidence={ECO:0000305\|PubMed:29717535}; CATALYTIC ACTIVITY: Reaction=CTP + H2O = CMP + diphosphate + H(+); Xref=Rhea:RHEA:27762, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:60377; EC=3.6.1.9; Evidence={ECO:0000269\|PubMed:29717535}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27763; Evidence={ECO:0000305\|PubMed:29717535}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GMP + diphosphate + H(+); Xref=Rhea:RHEA:29391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58115; EC=3.6.1.9; Evidence={ECO:0000269\|PubMed:29717535}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29392; Evidence={ECO:0000305\|PubMed:29717535}; CATALYTIC ACTIVITY: Reaction=UTP + H2O = UMP + diphosphate + H(+); Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9; Evidence={ECO:0000269\|PubMed:29717535}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29396; Evidence={ECO:0000305\|PubMed:29717535}; CATALYTIC ACTIVITY: Reaction=UDP-N-acetyl-alpha-D-glucosamine + H2O = N-acetyl-alpha-D-glucosamine 1-phosphate + UMP + 2 H(+); Xref=Rhea:RHEA:29547, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:57776, ChEBI:CHEBI:57865; Evidence={ECO:0000250\|UniProtKB:Q6DYE8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29548; Evidence={ECO:0000250\|UniProtKB:Q6DYE8}; CATALYTIC ACTIVITY: Reaction=P(1),P(3)-bis(5'-adenosyl) triphosphate + H2O = AMP + ADP + 2 H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000269\|PubMed:12846830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13894; Evidence={ECO:0000305\|PubMed:12846830}; CATALYTIC ACTIVITY: Reaction=P(1),P(4)-bis(5'-adenosyl) tetraphosphate + H2O = AMP + ATP + 2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215; Evidence={ECO:0000269\|PubMed:12846830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32040; Evidence={ECO:0000305\|PubMed:12846830}; CATALYTIC ACTIVITY: Reaction=P(1),P(5)-bis(5'-adenosyl) pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58450, ChEBI:CHEBI:62041, ChEBI:CHEBI:456215; Evidence={ECO:0000269\|PubMed:12846830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32052; Evidence={ECO:0000305\|PubMed:12846830}; CATALYTIC ACTIVITY: Reaction=P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GMP + GTP + 2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; Evidence={ECO:0000269\|PubMed:12846830}; CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000269\|PubMed:11342463, ECO:0000269\|PubMed:29717535, ECO:0000269\|PubMed:9344668};
Subellular location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:11342463, ECO:0000269\|PubMed:12846830}; Single-pass type II membrane protein {ECO:0000305\|PubMed:29717535}. Apical cell membrane {ECO:0000269\|PubMed:15072822}; Single-pass type II membrane protein {ECO:0000305\|PubMed:29717535}. Secreted {ECO:0000269\|PubMed:15072822}. Note=Detected at the cell surface of basophils (PubMed:11342463). Detected at the apical plasma membrane of bile duct cells (PubMed:15072822). Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells. {ECO:0000269\|PubMed:11342463, ECO:0000269\|PubMed:15072822}.
Tissues TISSUE SPECIFICITY: Detected on bile ducts in liver, and in blood serum (at protein level) (PubMed:15072822). Detected in prostate and uterus (PubMed:9344668). Detected on basophils, but not neutrophils (PubMed:11342463). {ECO:0000269\|PubMed:11342463, ECO:0000269\|PubMed:15072822, ECO:0000269\|PubMed:9344668}.
Structure SUBUNIT: Monomer and homodimer. {ECO:0000269\|PubMed:29717535}.
Post-translational modification PTM: N-glycosylated. N-glycosylation is necessary for normal transport to the cell membrane, but is not the apical targeting signal. {ECO:0000250\|UniProtKB:P97675}.
Target Relevance information above includes information from UniProt accession: O14638
The UniProt Consortium

Data

HPLC of Biotinylated Human ENPP-3 (48-157) Protein

The purity of Biotinylated Human ENPP-3 (48-157) is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Human ENPP-3 (48-157) Protein

Biotinylated Human ENPP-3 (48-157) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.