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anti-Human PKD2 Antibodies:
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Human Polyclonal PKD2 Primary Antibody for IHC (p), ELISA - ABIN543268
Watnick, He, Wang, Liang, Parfrey, Hefferton, St George-Hyslop, Germino, Pei: Mutations of PKD1 in ADPKD2 cysts suggest a pathogenic effect of trans-heterozygous mutations. in Nature genetics 2000
Show all 5 Pubmed References
Human Polyclonal PKD2 Primary Antibody for ELISA, WB - ABIN4346790
Fencl, Janda, Bláhová, Hríbal, Stekrová, Puchmajerová, Seeman: Genotype-phenotype correlation in children with autosomal dominant polycystic kidney disease. in Pediatric nephrology (Berlin, Germany) 2009
PKD2 and PKD1 genes are mutated in autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2.
this is the first report of autosomal dominant polycystic kidney disease complicated with aortic dissection caused by PKD2 mutation
this study reports the 3.6-angstrom cryo-electron microscopy structure of truncated human PKD1-PKD2 complex assembled in a 1:3 ratio.
newly identified sites for known mutations will facilitate the early diagnosis and prediction of prognosis in patients with ADPKD
This noticeable hot spot regions hold higher frequency (50%) of pathogenic / likely pathogenic genetic variants constituting single nucleotide variants than large deletion and insertion that actually represents only 41.08% of coding sequence of PKD2. Statistically significant association for IVS3-22AA genotype was observed with PKD, while association of IVS4+62C>T was found insignificant.
the PKD1/PKD2 mutation status differed by ethnicity, and the PKD1/PKD2 genotype may affect the clinical phenotype of autosomal dominant polycystic kidney disease
The novel pathogenic variant in c.637C> T in PKD2 is very interesting since they may represent Italian clusters.
Upregulation of miR-106b-5p or downregulation of PKD2 expression can cause A549/DDP cells to become considerably more sensitive to cisplatin. The results showed that miR-106b-5p enhanced the sensitivity of A549/DDP cells to cisplatin by targeting the expression of PKD2.
investigated the interaction network of human PKD2 in the cytosol and in Golgi-enriched subcellular protein fractions
SNX3-retromer complex regulates the surface expression and function of PC1 and PC2
We aimed to revisit PKD2 prevalence, clinical presentation, mutation spectrum, and prognosis through the Genkyst cohort. Patients with PKD2-related dominant polycystic kidney disease typically present with mild disease
Hyperactivation of the ERK pathway may be caused by down-regulation of PC-1 and PC-2 in lymphatic malformations, contributing to increased proliferation of lymphatic endothelial cells.
Annualized median liver growth rates were 1.68, 1.5 and 1.24% for PKD1-T, PKD1-NT and PKD2 mutations, respectively (P = 0.49), and remained unaffected by the ADPKD genotype when adjusted for age, gender and baseline HtLV.
Here, we review previous studies that connect the molecular properties of the domains of PC2 Cterm to distinct aspects of PC2 functions and regulation.
TRPP2 mutations are associated with autosomal dominant polycystic kidney disease.
Data show that in 82 (87.2%) of the patients, pathogenic mutations were detected in PKD1 (79.0%-92.5%), whereas in 12 (12.8%) patients pathogenic mutations were detected in PKD2 (7.5%-21.0%).
Two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
The structure of human PC2 in a closed conformation, solved by electron cryomicroscopy at 4.2-A resolution.
SNPs in and near PKD2 showed significant evidence of association in individual samples of black adults (rs17013735, P-value=0.0009) and white adults (rs11938025; P-value=0.0005; rs2725270, P-value=0.003).
Pancreatic cysts were more prevalent in patients with ADPKD with PKD2 mutation than in control subjects or patients with PKD1 mutation.
MAPK-15 is a ciliary protein required for PKD-2 localization and male mating behavior in Caenorhabditis elegans
acts as a major calcium-release channel in the endoplasmic reticulum in cells where rapid calcium signaling is required, and is essential in those excitable cells for rapid responses to stimuli (polycystin-2)
expressed in male-specific neurons, required for mating
Both general and cell-type-specific factors govern TRPP2/PKD-2 subcellular distribution by forming at least two steps involving somatodendritic and ciliary sorting decisions.
These data reveal that the STAM-Hrs complex, which down-regulates ligand-activated growth factor receptors from the cell surface of yeast and mammalian cells, also regulates the localization and signaling of a ciliary PC1 receptor-TRPP2 complex.
Results demonstrate that somatodendritic and ciliary targeting of PKD-2 requires the transmembrane region of PKD-2 and that the PKD-2 cytosolic termini regulate subcellular distribution and function.
11 mutants found with defects in the ciliary localization (cil) of C. elegans PKD-2, a transient receptor potential polycystin (TRPP) channel
Results show that Far Upstream Element-Binding Protein 1 Binds the 3' Untranslated Region of PKD2 to inhibit PKD2 translation, regulating zebrafish disease phenotypes associated with PKD2 knockdown
TRPP2 and TRPV4 are mechanosensitive channels in the endocardium.Oscillatory flow modulates mechanosensitive klf2a expression through trpv4 and trpp2 during heart valve development.
Intraciliary calcium oscillations depend on Pkd2 and are left-biased at the left-right organizer in response to ciliary motility.
TRPP2 utilizes TRPV4 to form a mechano- and thermosensitive molecular sensor in the cilium.[TRPP2]
Isolated pkd2 mutant hearts displayed impaired intracellular calcium cycling and calcium alternans. These results indicate heart failure in the pkd2 mutants.
PKD2 suppression inactivates CaMK-II in pronephric cells and cilia, whereas constitutively active CaMK-II restores pronephric duct formation in pkd2 morphants
Proper heart valve formation in zebrafish critically depends on protein kinase D2-histone deacetylase 5-Kruppel-like factor signaling.
Pkd1a/b and pkd2 interact to regulate extracellular matrix secretion or assembly, and that altered matrix integrity may be a primary defect underlying autosomal dominant polycystic kidney disease tissue pathologies.
PRKCSH functions as a chaperone-like molecule, which prevents endoplasmic reticulum-associated degradation of TRPP2.
atp-2, lov-1, and pkd2 act in the same molecular pathway.
The functions of polaris and pkd2 in LR patterning are conserved between zebrafish and mice and that Kupffer's vesicle
In zebrafish pkd2 is not responsible for the activation of spaw transcription, but is required for a mechanism to restrict spaw expression to the left half of the embryo. pkd2 also appears to play a role in the propagation of Nodal signals in the LPM.
role in the development of normal left-to-right asymmetry depends on endoplasmic reticulum localization
The flow-induced calcium signaling depends on the ciliary polycystin-2 calcium channel.
cloning and characterization of the PKD2 cDNA showing that the full-length gene (3370 bases) is highly expressed in kidney, with minimal expression in the liver
EGF may reduce the threshold of PKD2 activation by mechanical and other stimuli by releasing it from PIP(2)-mediated inhibition.
heteromeric cation channels comprised of the TRPP2 mutant and the TRPC3 or TRPC7 protein induce enhanced receptor-activated Ca(2+) influx that may lead to dysregulated cell growth in ADPKD
This gene encodes a member of the polycystin protein family. The encoded protein is a multi-pass membrane protein that functions as a calcium permeable cation channel, and is involved in calcium transport and calcium signaling in renal epithelial cells. This protein interacts with polycystin 1, and they may be partners in a common signaling cascade involved in tubular morphogenesis. Mutations in this gene are associated with autosomal dominant polycystic kidney disease type 2.
, autosomal dominant polycystic kidney disease type II protein
, transient receptor potential cation channel, subfamily P, member 2
, polycystic kidney disease 2 protein homolog
, polycystin 2
, polycystic kidney disease 2 homolog
, polycystic kidney disease 2 membrane protein
, cation channel
, polycystic kidney disease 2 (autosomal dominant) L homeolog
, Curly up
, Polycystic kidney disease 2 protein homolog
, Transient receptor potential cation channel subfamily P member 2
, curly up
, transient receptor potential cation channel subfamily P member 2
, polycystic kidney disease 2 (autosomal dominant)