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is richly expressed in the kidney, where it plays critical roles in the secretion, from the blood to urine, of clinically important drugs.
Our findings suggest that because OAT1 is capable of transporting d-luc, it can also be used to improve visualization and monitoring of luciferase-expressing cells.
SLC22A6 variants were not significantly associated with hyperuricemia and gout in a New Zealand Maori and Pacific cohort.
this is the first demonstration that Nedd4-1 regulates hOAT1 ubiquitination, expression, and transport activity through its WW2 and WW3 domains
both Nedd4-1 and Nedd4-2 are important regulators for hOAT1 ubiquitination, expression, and function
Uremic toxins, p-cresyl sulfate and indoxyl sulfate, are transported into endothelial cells by OAT1/OAT3.
high capacity p-cresyl sulfate trasnporter
OAT1 and NaDC3 in the basolateral membrane and OAT4 in the luminal membrane of proximal tubule cells are responsible for the avid renal secretion of N-carbamoylglutamate.
BCL6 constitutes a promising candidate gene for the regulation of human OAT1 transcription
Clopidogrel/clopidogrel carboxylate are weak inhibitors of OAT1.
The results confirmed that OAT1, OAT3, OCT2, MATE1, and MATE2-K were coexpressed in tubular epithelial cells.
transport of xanthurenic acid by OAT1 and OAT3
PKC isoform PKCalpha was responsible for OAT1 ubiquitination.
It was shown that human OAT3 and OAT1 cannot be involved in the renal extraction of glutathione from blood, but OAT1 could support intracellular glutathione synthesis by taking up cysteinyl glycine.
Both hOAT1 and hOAT3 markedly stimulated the uptake of kynurenic acid into oocytes.
High urine OAT1 and OAT3 and low OAT4 is associated with early reversible proximal tubular damage.
The data reveal alpha-ketoglutarate as a common high-affinity substrate of NaDC3, OAT1, and OAT3
Intergenic polymorphism rs10792367 between OAT1 and OAT3 is not associated with hypertension, but appears to be involved in between-individual variations in antihypertensive responses to hydrochlorothiazide.
Our results are the first to highlight the central role of TM 12 in maintaining the stability and in promoting the maturation efficiency of hOAT1.
results suggest that genetic polymorphisms may not be a significant contributing factor to variations in the hOAT2 expression or hOAT2 transport activity
Its anti-hyperuricemic mechanisms may be ascribed to its inhibition of XOD and its up-regulation of organic anion transporter 1 (OAT1) and down-regulation of glucose transporter 9 (GLUT9).
It is the key assembly for uric acid secretion through kidney.
OCT2-independent pathway of cisplatin-induced renal injury that is mediated by the organic anion transporters OAT1 and OAT3, is reported.
An Organic Anion Transporter 1 (OAT1)-centered Metabolic Network.
Arsenic and mercury containing traditional Chinese medicine (Realgar and Cinnabar) probably induce kidney damage through inhibiting several members of the organic anion transporters (such as OAT1 and OAT3).
OAT1-deficient mice showed abnormal LTP and higher spine numbers but with a much lesser maturity extent.
At the protein level, mOat3 and mOat1 exhibit sex-dependent expression with an opposite pattern; mOat3 is female dominant due to androgen inhibition, while mOat1 is male dominant due to androgen stimulation.
Oat1 potentially plays a major role in the rate limiting step in the uptake and excretion of putative toxic metabolites
acute kidney injury by HgCl(2) was found to be mediated mainly by Oat1.
functional differences in the relative importance of OAT1 and OAT3 in antiviral handling in developing and mature tissue
the ontogenic pattern of expression of OAT1 and OAT3 in the differentiating proximal tubules suggests that both transporters may function in the S2 segment in the fetus
Although all cysteine mutants of mOAT1 were sensitive to the inhibition by PCMBS, C49A was less sensitive than the wild-type mOAT1, suggesting that the modification of Cys49 may play a role in the inhibition of mOAT1 by PCMBS.
analysis of physiological substrates of OAT1
the substrate binding preferences and transport function of olfactory organic anion transporter, Oat6, in comparison with the more broadly expressed transporter, Oat1
The constitutive expression of OAT1 in the kidney is regulated by both HNF1alpha and HNF1beta.
despite sharing close overall sequence homology, Oat1, Oat3, and Oat6 have signficantly different binding pockets
data demonstrate that PKCzeta activation up-regulates OAT1 and OAT3 function, and that protein-protein interactions play a central role controlling these two important renal drug transporters
Oat1, Oat3, and Oat6 function largely in organic anion transport but also bind and transport organic cations.
The protein encoded by this gene is involved in the sodium-dependent transport and excretion of organic anions, some of which are potentially toxic. The encoded protein is an integral membrane protein and may be localized to the basolateral membrane. Four transcript variants encoding four different isoforms have been found for this gene.
, organic anion transporter 1
, para-aminohippurate transporter
, renal organic anion transporter 1
, solute carrier family 22 member 6
, kidney-specific transport protein
, novel kidney transcript
, organic cationic transporter-like 1
, solute carrier family 22 (organic anion transporter), member 6
, Solute carrier family 22 member 6
, solute carrier family 22, member 6
, organic cation transporter 1-B
, renal organic anion transporter 1-B
, solute carrier family 22 member 6-B
, putative organic anion transporter
, LOW QUALITY PROTEIN: solute carrier family 22 member 6