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Human Polyclonal PKD1 Primary Antibody for IF (p), IHC (p) - ABIN678083
Chiou, Sang, Cheng, Ho, Wang, Pan: Peracetylated (-)-epigallocatechin-3-gallate (AcEGCG) potently prevents skin carcinogenesis by suppressing the PKD1-dependent signaling pathway in CD34+ skin stem cells and skin tumors. in Carcinogenesis 2013
Show all 4 Pubmed References
Analysis of polycystin-1 (PC1) indicates that humans, but not mice, have a smaller than expected protein product, which we call Trunc_PC1. The findings show that Trunc_PC1 is the protein product of abnormal differential splicing across introns 21 and 22 and that 28.8%-61.5% of PKD1 transcripts terminate early.
We found that the inhibitory Galphai3 protein selectively bound to the G-protein-binding domain on the C-terminus of PC1. The dissociation of Galphai3 upon cleavage of PC1 increased TRPC4 activity
Significant phenotypic differences were observed among the various types of PKD1 mutations in Han Chinese patients with autosomal dominant polycystic kidney disease.
New reports reveal the emergence of polycystins (polycystin-1, PC1; and polycystin-2, PC2) as key proteins that facilitate the transduction of mechano-induced signals in various clinical entities besides polycystic kidney disease, such as cancer, cardiovascular defectsbone loss, and deformations, as well as inflammatory processes like psoriasis. [review]
A Czech family with autosomal dominant polycystic kidney disease is reported to have a co-inheritance of PKD1 and PKD2 pathogenic variants.
structure of the complex of PC1 and PC2 and its interaction domains
Study highlighted the clinical characteristics of individuals with autosomal dominant polycystic kidney disease (ADPKD) in Tunisia. Direct sequencing revealed three novels mutations i.e. p.S463C exon 7; c. c.11156+2T>C IVS38 and c.8161-1G>A IVS22 and two previously reported c.1522T>C exon 7 and c.412C>T exon 4 mutations in the PKD1 gene.
show that PC1 and PC2 are expressed in radial glial cells of the developing mouse cerebral cortex during neurogenesis
Involvement of PC1-regulated eIF2alpha phosphorylation and a PKR-eIF2alpha pathway in cell apoptosis may be an important part of the mechanism underlying ADPKD pathogenesis.
Results found PC1 exhibiting decreased expression in human psoriatic lesions. In vitro, PC1 downregulation activates the mTOR pathway in keratinocytes in an ERK-dependent manner
A novel splicing mutation in the PKD1 gene causes autosomal dominant polycystic kidney disease in a Chinese family.
Novel mutations of PKD1 and PKD2 genes in Chinese patients suffering from autosomal dominant polycystic kidney disease and seeking assisted reproduction have been described.
Identification of PKD1 and PKD2 gene variants in a cohort of 125 Asian Indian patients of ADPKD.
Expression of PC1DeltaL and PC2 complexes in transfected CHO cells failed to support PC2 channel activity, suggesting that the role of PC1 is to activate G-protein signaling to regulate the PC1/PC2 calcium channel.
Our study has identified PKD1 as a frequently downregulated gene in HNSCC, and functionally, under certain cellular context, may play a role in GRP/bombesin-induced oncogenesis in HNSCC.
Data found that MTA1 is a PKD1-interacting substrate, and that PKD1 phosphorylates MTA1, supports its nucleus-to-cytoplasmic redistribution and utilizes its N-terminal and kinase domains to effectively inhibit the levels of MTA1 via polyubiquitin-dependent proteosomal degradation.
Two novel mutations, c.6953_6977del and c.10937T>G (p.Val3646Gly) of the PKD1 gene are associated with the polycystic kidney disease.
this study reports the 3.6-angstrom cryo-electron microscopy structure of truncated human PKD1-PKD2 complex assembled in a 1:3 ratio.
VEGF/PKD-1 signaling axis increases angiogenic and arteriogenic gene expression. These studies suggest that the axis may regulate arteriolar differentiation through changing microvascular endothelial cells gene expression.
The novel frameshift mutations reported by this study are p. Q1997X, P. D73X and p. V336X.
PC1 is involved in renal Mg(2+), Ca(2+), and water handling and its dysfunction, resulting in a systemic electrolyte imbalance characterized by low serum electrolyte concentrations in mouse model for autosomal dominant polycystic kidney disease.
polycystins and TAZ integrate at the molecular level to reciprocally regulate osteoblast and adipocyte differentiation, indicating that the polycystins/TAZ complex may be a potential therapeutic target to increase bone mass.
Pkd1DeltaL/DeltaL mice were embryo-lethal suggesting that DeltaL is a functionally null mutation. Kidney-specific Pkd1DeltaL/cond mice were born but developed severe, postnatal cystic disease.
increased activation of selected genes in renal epithelial cells early upon Pkd1 gene disruption may disturb the balance in signaling and may contribute to cyst formation.
Results indicate that PKD1 inactivation underlies excitotoxicity-induced neuronal death and suggest that PKD1 inactivation may be critical for the accumulation of oxidation-induced neuronal damage during aging and in neurodegenerative disorders.
PKD1 contributes to the osteoblast differentiation and bone development via elevation of osteoblast markers through activation of STAT3 and p38 MAPK signaling pathways.
PKD1 mediates the PKC effects on KV11.1 and we found that PKD targets S284 in the N-terminus of the channel.
PC1/3 deficiency was associated with increased expression of melanocortin receptors and PRCP (prolylcarboxypeptidase, a catabolic enzyme for alpha-melanocyte stimulating hormone (alphaMSH)), and reduced adrenocorticotropic hormone secretion. We conclude that the obesity accompanying PCSK1 deficiency may not be primarily due to alphaMSH deficiency.
Mutations in PKD1 is associated with autosomal dominant polycystic kidney disease.
critical functions of PC1 are regulated by its ability to sense cytosolic calcium levels via binding to calmodulin
cortactin binds to E-cadherin, and that a posttranslational modification of cortactin, RhoA-induced phosphorylation by protein kinase D1 (PKD1; also known as PRKD1) at S298, impairs adherens junction assembly and supports their dissolution.
Galpha12 is required for the development of kidney cysts induced by Pkd1 mutation in mouse autosomal dominant polycystic kidney disease.
PAK-mediated phosphorylation of PKD1 at Ser203 triggers its membrane dissociation and subsequent entry into the nucleus, thereby regulating the phosphorylation of PKD1 nuclear targets, including class IIa histone deacetylases.
kd1 mutant mice have transcriptional profiles consistent with changes in lipid metabolism and distinct metabolite and complex lipid profiles in kidneys. .. cells lacking Pkd1 have an intrinsic fatty acid oxidation defect and that manipulation of lipid content of mouse chow modifies cystic disease.
Polycystin 1 was overexpressed in M1 cells, no increase in any of these parameters was detected
detected a marked increase in the localization of beta-catenin in the nucleus of crypt epithelial cells in the ileum of PKD1
PKD1 phosphorylates AMPKalpha2 at Ser485/491, thus diminishing AMPK activity.
These data potentially explain the severe renal manifestations of the tuberous sclerosis/polycystic kidney disease contiguous gene syndrome and open new perspectives for the use of mTOR inhibitors in PKD.
novel protein complex composed of Rabep1, GGA1 and Arl3 is responsible for the sorting and targeting of the polycystin 1 andpolycystin 2 to the cilium.
Polycystin-1 regulation of the microtubule cytoskeleton impacts on the turnover rates of focal adhesions in migrating cells and we link all these properties to the capability of PC-1 to regulate the activation state of Focal Adhesion Kinase.
This gene encodes a member of the polycystin protein family. The encoded glycoprotein contains a large N-terminal extracellular region, multiple transmembrane domains and a cytoplasmic C-tail. It is an integral membrane protein that functions as a regulator of calcium permeable cation channels and intracellular calcium homoeostasis. It is also involved in cell-cell/matrix interactions and may modulate G-protein-coupled signal-transduction pathways. It plays a role in renal tubular development, and mutations in this gene cause autosomal dominant polycystic kidney disease type 1 (ADPKD1). ADPKD1 is characterized by the growth of fluid-filled cysts that replace normal renal tissue and result in end-stage renal failure. Splice variants encoding different isoforms have been noted for this gene. Also, six pseudogenes, closely linked in a known duplicated region on chromosome 16p, have been described.
autosomal dominant polycystic kidney disease 1 protein
, polycystic kidney disease-associated protein
, polycystin 1
, transient receptor potential cation channel, subfamily P, member 1
, autosomal dominant polycystic kidney disease 1 protein homolog
, polycystic kidney disease 1 homolog; polycystin-1
, polycystic kidney disease 1 (autosomal dominant)
, polycystic kidney disease protein 1