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ENTPD5 / CD39L4 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | O75356 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 48kDa |
| Dilution | IHC-P (10 µg/ml), WB (1:500-1:3000), |
| Gene ID | 957 |
|---|---|
| Other Names | Ectonucleoside triphosphate diphosphohydrolase 5, NTPDase 5, 3.6.1.6, CD39 antigen-like 4, ER-UDPase, Guanosine-diphosphatase ENTPD5, GDPase ENTPD5, 3.6.1.42, Nucleoside diphosphatase, Uridine-diphosphatase ENTPD5, UDPase ENTPD5, ENTPD5, CD39L4, PCPH |
| Target/Specificity | Human ENTPD5. Predicted cross-reactivity based on amino acid sequence homology: mouse (88%), rat (86%). |
| Reconstitution & Storage | Aliquot and store at -20°C. Minimize freezing and thawing. |
| Precautions | ENTPD5 / CD39L4 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ENTPD5 (HGNC:3367) |
|---|---|
| Function | Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (PubMed:15698960, PubMed:10400613). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP- glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity). |
| Cellular Location | Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted |
| Tissue Location | Expressed in adult liver, kidney, prostate, testis and colon. Much weaker expression in other tissues |
| Volume | 50 µl |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Uridine diphosphatase (UDPase) that promotes protein N- glycosylation and ATP level regulation. UDP hydrolysis promotes protein N-glycosylation and folding in the endoplasmic reticulum, as well as elevated ATP consumption in the cytosol via an ATP hydrolysis cycle. Together with CMPK1 and AK1, constitutes an ATP hydrolysis cycle that converts ATP to AMP and results in a compensatory increase in aerobic glycolysis. The nucleotide hydrolyzing preference is GDP > IDP > UDP, but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. Plays a key role in the AKT1-PTEN signaling pathway by promoting glycolysis in proliferating cells in response to phosphoinositide 3-kinase (PI3K) signaling.
References
Chadwick B.P.,et al.Genomics 50:357-367(1998).
Recio J.A.,et al.Mol. Carcinog. 27:229-236(2000).
Murphy-Piedmonte D.M.,et al.Biochim. Biophys. Acta 1747:251-259(2005).
Heilig R.,et al.Nature 421:601-607(2003).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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