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The protein encoded by SLC20A1 is a sodium-phosphate symporter that absorbs phosphate from interstitial fluid for use in cellular functions such as metabolism, signal transduction, and nucleic acid and lipid synthesis. Additionally we are shipping SLC20A1 Antibodies (34) and and many more products for this protein.
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Cysteine substitution at some sites also altered the apparent affinity for Pi and cation (Na(+)/Li(+)) and substrate (phosphate/arsenate) selectivity, further underscoring the importance of this linker in defining PiT-1 transport characteristics.
Targeted sequencing of two candidate genes, SLC20A1 and SLC15A4, of the solute carrier membrane transport protein family in 200 additional patients demonstrated two further variants predicted as damaging for combined hormone deficiency.
Overexpression of SLC20A1 is associated with Estrogen Receptor-positive Breast Cancer.
indoxyl sulfate promotes Pit-1 expression in part by activation of the JNK pathway in vascular smooth muscle cells
Ox-LDL induces an osteogenic change in human aortic valve interstitial cells marked by the induction of PiT-1.
Overexpression of SLC20A1 promotes apoptosis and mineralization by altering the level of Akt-1.
Allelic variations in SLC20A1 were associated with the levels of Sodium-lithium countertransport.
the human PiT2 histidine, H(502), and the human PiT1 glutamate, E(70),--both conserved in eukaryotic PiT family members--are critical for P(i) transport function
Identification of a novel transport-independent function of PiT1/SLC20A1 in the regulation of TNF-induced apoptosis.
propose that region A of Pit1 confers competence for viral entry by influencing the topology of the authentic binding site in the membrane and hence its accessibility to a viral envelope protein
Two highly conserved glutamate residues critical for sodium-dependent phosphate transport are revealed by uncoupling transport function from retroviral receptor function.
Our results link low-grade IL-8-mediated cartilaginous inflammation in OA to altered chondrocyte differentiation and disease progression through PiT-1 expression and sodium-dependent Pi uptake mediated by CXCR1 signaling.
Phosphate uptake through Pit-1 is essential for vascular smooth muscle cell calcification and phenotypic modulation in response to elevated phosphate.
Results describe the characterization of transport mechanisms and determinants critical for sodium-dependent phosphate symport of the PiT family paralogs human PiT1 and PiT2.
Analysis of kinetics and substrate specificity of SLC20A1.
An overexpression of Pit-1 seems to play a key role in the formation of soft tissue calcification in Werner syndrome.
PiT1 depletion markedly reduces cell proliferation, delays cell cycle, and impairs mitosis and cytokinesis.
The protein encoded by this gene is a sodium-phosphate symporter that absorbs phosphate from interstitial fluid for use in cellular functions such as metabolism, signal transduction, and nucleic acid and lipid synthesis. The encoded protein is also a retroviral receptor, causing human cells to be susceptible to infection by gibbon ape leukemia virus, simian sarcoma-associated virus, feline leukemia virus subgroup B, and 10A1 murine leukemia virus.
solute carrier family 20 (phosphate transporter), member 1
, sodium-dependent phosphate transporter 1
, solute carrier family 20 member 1
, sodium-dependent phosphate transporter 1-B
, solute carrier family 20 member 1-B
, gibbon ape leukemia virus receptor 1
, leukemia virus receptor 1 homolog
, phosphate transporter 1
, feline leukemia virus subtype-B receptor
, leukemia virus-b receptor