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Validated All-in-One™ qPCR Primer for PLD2(NM_002663.4) Search again
Product ID:
HQP013244
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
PLD1C
Gene Description:
phospholipase D2
Target Gene Accession:
NM_002663.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
Phosphatidylcholine (PC)-specific phospholipases D (PLDs; EC 3.1.4.4) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM].
Gene References into function
- activation of phospholipases D1 and D2 by S1P regulates the phosphorylation of extracellular-signal-regulated kinase and IL-8 secretion in Beas-2B cells
- localizes to the plasma membrane of mast cells; stimulated by oleic acid
- PLD2 activity is directly regulated by ADP-ribosylation factor 4, and this ARF4-mediated PLD2 activation stimulates AP-1-dependent transcription in the EGF-induced cellular response
- PLD is regulated py phosphoinositides through the PH domain and the polybasic motif
- PLD2 may play a key role in the regulation of agonist-induced endocytosis of the mu-opioid receptor
- Phospholipase D(2) gene is a susceptibility locus for colorectal cancer in Japanese individuals.
- elevated PLD activity generates survival signals allowing cells to overcome default apoptosis programs
- PLD isozymes stimulate cell growth by repressing expression of p21 gene
- phospholipase D2 was enriched in caveolae; PLD2 could be involved in MEK/ERK signaling cascades that are induced by the VEGF/VEGFR-2/PKC-delta pathway in endothelial cells
- PLD2 functions at the plasma membrane to facilitate endocytosis of the angiotensin II type 1 receptor.
- The phospholipase D2 possesses a PH domain, activation by phosphatidylinositol 4,5-disphosphate (PIP2) involves binding to a conserved cluster of basic residues.
- Translocation of PLD2 to EGF-induced membrane ruffles has been observed in HeLa cells when coexpressed with PIP kinase Ialpha.
- phospholipase D isozymes mediate EGCG-induced COX-2 expression through PKC and p38 in immortalized astroglial line and normal astrocyte cells
- findings provide the first description of a mechanism for activation phospholipase D2 in a physiological setting and of a role for Fyn and Fgr in Fc epsilon RI-mediated signaling.
- an increase in local membrane monomeric tubulin concentration inhibits PLD2 activity
- ANP recruits a signal pathway associated with p38 MAPK, NHE-1 and PLD responsible for ROS production, suggesting a possible role for ANP as novel modulator of ROS generation in HepG2 cells
- Phospholipase D2 (PLD2) enhances PKCzeta activity through direct interaction in a lipase activity-independent manner.
- EWS-Fli1 may play a role in the regulation of PDGF-induced tumor proliferation-signaling enzymes via PLD2 expression in Ewing sarcoma cells
- intracellular unsaturated acyl-CoA derivatives destabilize ABCA1 by activating a PLD2 signaling pathway
- These results suggest that intact phosphorylation sites within the MARCKS ED are required for PLD activation and influence both membrane-cytoskeletal organization and cell viability.
- Y(169) & Y(179) are in 2 consensus sites in PLD2 mediating SH2 interaction with Grb2. They are needed for recruiting Sos, but only overexpression of the PLD2 Y179F mutant resulted in more Ras activity, p44/42(Erk) phosphorylation & enhanced DNA synthesis
- PLD functions as a GTPase activating protein (GAP) through its phox homology domain (PX), which directly activates the GTPase domain of dynamin and increased epidermal growth factor receptor (EGFR) endocytosis at physiological EGF concentrations.
- Data show that the G-->A (Gly901Asp) mutation of the human PLD2 gene results in catalytic inactivation of the encoded protein.
- demonstration of the involvement of PLD1 and PLD2 and its enzymatic activity toward chemokines in the key physiologic process of leukocyte migration
- gene expression is increased by EWS.Fli-1 and FLI-1 by binding to an erythroblast transformation-specific domain of the PLC2 promoter
- Our findings establish a crucial role for PLD2 in the coupling of extracellular signals to Sos-mediated Ras activation, and provide new insights into the spatial coordination of this activation event.
- Thus, LFA-1 acts through PLD2 to reshape the pattern of Ras activation downstream of the TCR
- Plays a major role in promoting HIV-1 long terminal repeat transactivation and virus replication.
- These results demonstrate for the first time that PLD1 and PLD2 isozymes enhance cobalt chlorde-induced COX-2 expression through differential signaling pathways in astroglioma cells.
- Elevated phospholipase D2 is associated with colorectal carcinoma
- Data suggest that recombinant human phospholipase D2 alone cannot induce apoptosis in HL-60 cells, but it can potentiate the apoptosis of HL-60 cells induced by camptothecin.
- These findings indicate the involvement of phospholipase D activation in hBD-2 up-regulation in gingival epithelial cells.
- Protein kinase C-epsilon regulates sphingosine 1-phosphate-mediated migration of human lung endothelial cells through activation of phospholipase D2, protein kinase C-zeta, and Rac1
- depletion of phospholipase D2 inhibited motility more severely, essential for the maintenance of keratocyte-like locomotion of NBT-II cells, presumably by regulating the actin cytoskeleton.
- Data suggest that PLD2 is an early player upstream of the Ras-ERK1/2-IL-2 pathway in T-cells via phosphatidic acid and diacylglycerol production.
- we present evidence for the presence of both PLD1 and PLD2 in platelets and indicate a role in platelet activation.
- Expression of active PLD2 enhances processes favorable to lymphoma cell metastasis, whereas expression of inactive PLD2 inhibits metastasis.
- The study results suggest that PLD2 is a new substrate of Cdk5 and that the phosphorylation of PLD2 by Cdk5 is involved in epidermal growth factor-dependent insulin secretion.
- Phospholipase D2 is cleaved at two or three sites in the front of N-terminus and maintained anti-apoptotic potency in spite of its cleavage during apoptosis.