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Validated All-in-One™ qPCR Primer for PLD1(NM_002662.4) Search again
Product ID:
HQP013243
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CVDD, CVDP1
Gene Description:
phospholipase D1
Target Gene Accession:
NM_002662.4(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. A range of agonists acting through G protein-coupled receptors and receptor tyrosine kinases stimulate this hydrolysis. PC-specific PLD activity has been implicated in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis (Hammond et al., 1995 [PubMed 8530346]).[supplied by OMIM].
Gene References into function
- alpha-Synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells
- regulation of polymorphonuclear leukocyte degranulation and oxidant production
- Detecting protein-phospholipid interactions. Epidermal growth factor-induced activation of phospholipase D1b in situ
- binding of the Rho family member Cdc42 to PLD1 and the subsequent stimulation of its enzymatic activity are distinct events
- PLD1 is threonine-phosphorylated in human-airway epithelial cells by a PKCdelta and src dependent mechanism
- activation of phospholipases D1 and D2 by S1P regulates the phosphorylation of extracellular-signal-regulated kinase and IL-8 secretion in Beas-2B cells
- activity regulated by actin in a polymerization-dependent, isoform-specific manner
- activated by ADP-ribosylated RhoA
- 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 D confers rapamycin resistance in human breast cancer cells. Elevated PLD activity in MCF-7 cells also caused rapamycin resistance for S6 kinase phosphorylation and serum-induced Myc expression.
- protein kinase C alpha associates with phospholipase D1 and enhances basal phospholipase D activity in a protein phosphorylation-independent manner in melanoma cells, which contributes to the cell's high invasive potential.
- results indicate that PKCdelta inhibits TPA-induced PLD1 activation mediated by PKCalpha through the association with PLD1
- isoenzyme PLD1 is stimulated by phorbol ester and requires ADP-ribosylation factor, protein kinase C and Rho proteins for full activity
- phospholipase D causes translocation of protein kinase C (PKC)betaII but not PKCbetaI to a juxtanuclear subset of recycling endosomes
- phospholipase D isozymes mediate EGCG-induced COX-2 expression through PKC and p38 in immortalized astroglial line and normal astrocyte cells
- PLD1 activity by regulating phosphatidic acid formation controls the early signals initiated by FcepsilonRI aggregation that lead to mast cell degranulation.PH
- importance of phospholipase D in the oncogenic ability of Ras
- phospholipase D suppresses protein phosphatase 2A and is involved in the mTOR survival pathway in the transformation of human cells
- PLD1 is activated by exclusion from lipid rafts and that this activation conveys antiproliferative signals in lymphoid cells
- 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.
- overexpression of PLD1 decreases, and down-presenilin 1, through its loop region, binds to phospholipase D1 (PLD1), thereby recruiting it to the Golgi/trans-Golgi network
- adhesion stimulates PLD activity, and that PLD1 regulates the initial stages of phagocyte adhesion
- endogenous PLD1 is a critical factor in the organization of the actin-based cytoskeleton, with regard to cell adhesion and migration
- 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.
- demonstration of the involvement of PLD1 and PLD2 and its enzymatic activity toward chemokines in the key physiologic process of leukocyte migration
- PLD1 may play a crucial role in collagen type I production through mTOR signaling in human dermal fibroblast.
- We show that human PLD1b (hPLD1b) is an actin-binding protein and the N-terminus is predominantly involved in this interaction.
- TNFalpha/CHX-induced cell death was significantly lowered in cells overexpressing PLD1
- isoform selective Arf/PLD interaction and not Arf/PtdIns4P5K will be the critical trigger in the formation of distinct, optimal triples of Arf/PLDs/PtdIns4P5Ks
- Our results indicate a possible role for novel PKC isoforms in the regulation of P2X(7)-mediated PLD activity.
- VDR and retinoid X receptor alpha (RXRalpha) binds to the VDRE and increases PLD1 gene expression in HaCaT cells.
- 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.
- PLD control over expression of the Mac-1 activation epitope is critical for neutrophil migration to fMLP but not C5a.
- PLD1 and phospho-mTOR are coexpressed in a subset of phospho-Akt-negative breast carcinomas.
- phospho-cofilin by its stimulatory effect on PLD1 may control a large variety of cellular functions.
- These findings indicate the involvement of phospholipase D activation in hBD-2 up-regulation in gingival epithelial cells.
- These results suggest that elevated expression and activity of PLD attenuate phorbol myristate acetate-induced Egr-1 expression via PI3K pathway.
- Depletion of phospholipase D1 by RNA interference reduced the velocity of the migration,of NBT-II cells.
- the critical role of PLD1 in the intracellular signaling cascades initiated by TNF-alpha and its functional role for coordinating the signals to inflammatory responses.
- we present evidence for the presence of both PLD1 and PLD2 in platelets and indicate a role in platelet activation.
- Phospholipase D activity regulates integrin-mediated cell spreading and migration by inducing GTP-Rac translocation to the plasma membrane
- PLD1 is required for Rheb activation of the mTOR pathway.
- a role for PKA in the regulation of thrombin-induced PLD1 activity and translocation in platelets.
- These data have identified a novel regulatory domain in PLD1.
- Cleavage of PLD1 by caspases promotes apoptosis via modulation of the p53-dependent cell death pathway.
- Phospholipase D1 is cleaved at one internal site and is significantly decreased during apoptosis.
- different mechanisms appear to control the agonist-induced secretion of von Willebrand factor and tissue-type plasminogen activator, with only the former requiring PLD1