Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Mouse (Murine) Antibodies:
anti-Rat (Rattus) Antibodies:
Go to our pre-filtered search.
Human Monoclonal GPLD1 Primary Antibody for IHC (fro), ELISA - ABIN532654
Gregory, Kraemer, Zürcher, Gentinetta, Rohrbach, Brodbeck, Andres, Ziemiecki, Bütikofer: GPI-specific phospholipase D (GPI-PLD) is expressed during mouse development and is localized to the extracellular matrix of the developing mouse skeleton. in Bone 2005
Show all 3 Pubmed References
computational study suggests that although curcumin to some extent binds with Tp receptor, yet the inhibition of Arf6GDP to Arf6GTP conversion appeared to be an important mechanism by which curcumin inhibits U46619-induced increase in PLD activity in PASMCs.
Study discovered novel and independent associations of prediabetes and related traits with MASP1, and some evidence for associations with THBS1, GPLD1 and ApoA-IV, suggesting a role for these proteins in the pathophysiology of type 2 diabetes.
c-Myc influences GPI-AP signaling transcriptionally and posttranslational and represses GPI-AP anti-proliferative signaling in tumors
An observed increase in PLD activity was mediated through boosting the binding of PLD with dynamin which in turn facilitated fibronectin-induced cell spreading.
Low aggressive MCF-7 breast cancer cells have low endogenous PLD enzymatic activity and cell invasion, concomitant with high expression of miR-203, -887, and -3619 and miR-182 and miR-182.
suggest that the down-regulation of GPI-PLD protein may be involved in prion propagation in the brains of prion diseases
our findings showed that ANRIL is an lncRNA responsible in anti-tumorigenesis caused by PLD inhibition and combined incorporation of ANRIL into PLD inhibition-induced anti-tumorigenic signaling network
AMPK suppresses PLD activity, and PLD suppresses AMPK via mTOR.
Functional regulation of phospholipase D expression in cancer and inflammation.
Phospholipase D and the maintenance of phosphatidic acid levels for regulation of mammalian target of rapamycin (mTOR).
At the cellular level, PLD and its reaction product, phosphatidate, interact with a large number of protein partners that are directly related to the actin cytoskeleton and cell migration.
PLD1 and PLD2 mutants inhibit very-low-density lipoprotein-induced aldosterone production in HAC15 cells.
This study indicated that PLD participates in the same signaling pathway in this breast cancer cell line.
genetic variation of GPLD1 appears to associate with circulating glycosylphosphatidylinositol-specific phospholipase D levels
The mRNA expression and activity of GPI-PLD in de novo and refractory or relapsed acute myeloid leukemia patients are obviously higher than those in normal controls.
This study revealed the novel mechanism of bleomycin-induced redox-sensitive activation of phospholipase D leading to the generation of phosphaticid acid.
The role of phospholipase D in the transport of VAT1 to plasma membranes and in phosphatidic acid metabolism in neutrophils is reported.
In human ovarian cancer cell lines, GPI-PLD mRNA expression correlated with GPI-PLD enzyme activity and with the shedding of the GPI-anchored tumor and prognostic markers, urokinase receptor and CA125, from the cell surface.
increased serum glycosylphosphatidylinositol-specific phospholipase D is associated with insulin resistance in a cohort with a wide range of insulin sensitivity
identified as component of human trypanosome lytic factor 1 (TLF1)
Overexpressing GPI-PLD in an insulinoma cell line enhanced glucose-stimulated insulin secretion, suggesting that enhanced insulin secretion in vivo may have contributed to the improved glucose tolerance.
GPI-PLD expression was significantly increased in highly malignant. H-ras-transfected murine bladder carcinoma cells as compared to the low malignant, non-transfected parental cells.
His29, His125, His133 and His158 are required for GPI-PLD catalytic activity
Glycosylphosphatidylinositol-specific phospholipase D influences triglyceride-rich lipoprotein metabolism.
Results suggest that cell-specific Gpld1- or peptidase-dependent pathways for prostasin secretion may control prostasin functions in a tissue-specific manner.
PLD plays an important role in inflammatory responses and could be involved in a mechanism for the regulation of endothelial barrier function during hyperoxic lung injury
Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by a glycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by this gene is a GPI degrading enzyme. Glycosylphosphatidylinositol specific phospholipase D1 hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans, thereby releasing the attached protein from the plasma membrane.
glycosylphosphatidylinositol specific phospholipase D1
, phosphatidylinositol-glycan-specific phospholipase D-like
, glycosylphosphatidylinositol specific phospholipase d1
, GPI-specific phospholipase D
, PI-G PLD
, glycoprotein phospholipase D
, phosphatidylinositol-glycan-specific phospholipase D
, glycosyl-phosphatidylinositol-specific phospholipase D
, glycosylphosphatidylinositol phospholipase D