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Amino Acid Transporter

Amino Acid Transporters are membrane-bound proteins that facilitate the movement of amino acids across biological membranes.
They play a crucial role in cellular metabolism, nutrient uptake, and signaling pathways.
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Most cited protocols related to «Amino Acid Transporter»

1
Transporter Substrate Specificity Prediction
We collected from the SwissProt UniProt database (release 2013_03) 10,780 transporter, carrier, and channel proteins that were well characterized at the protein level and had clear substrate annotations [15] (link), [16] (link). We removed sequences that were fragmented. We also removed sequences annotated with more than two substrate specificities and biological function annotations that were based solely on sequence similarity. We manually curated the biological function annotations from the remaining sequences and compiled a total of 1,110 membrane transport protein sequences in which only one transporting substrate has been reported in the literature. We removed 210 sequences that showed greater than 70% similarity using CD-HIT software [17] (link) (see Figure S1 for details about the data compilation and curation processes). The 900 remaining transporter sequences were then divided into seven major classes of transporters based on their substrate specificity: 85 amino acid/oligopeptide transporters, 72 anion transporters, 296 cation transporters, 70 electron transporters, 85 protein/mRNA transporters, 72 sugar transporters, and 220 other transporters. We also compiled 660 non-transporters as an extra class of control proteins in our model development process by randomly sampling all the proteins in UniProt release 2013_03 excluding the 10,780 transporters.
We further divided the 1,560 compiled proteins into two datasets: 1) the main dataset, which consisted of 70 amino acid transporters, 60 anion transporters, 260 cation transporters, 60 electron transporters, 70 protein/mRNA transporters, 60 sugar transporters, 200 other transporters, and 600 non-transport proteins for a total of 1,380 proteins; and 2) an independent dataset, which consisted of 15 amino acid transporters, 12 anion transporters, 36 cation transporters, 10 electron transporters, 15 protein/mRNA transporters, 12 sugar transporters, 20 other transporters, and 60 non-transport proteins for a total of 180 proteins (see Table S1 for a detailed dataset partition; all the sequences are available on our TrSSP web server at http://bioinfo.noble.org/TrSSP/). We applied a five-fold cross-validation schema on the 1,380 proteins in the main dataset to develop our SVM models. The performance of these SVM models was further tested and validated on the independent dataset of 180 proteins. To evaluate the prediction accuracy of the models for each class of proteins, proteins within the same class were considered a positive predictor and proteins from the remaining classes were considered a negative predictor.
Mishra N.K., Chang J, & Zhao P.X. (2014). Prediction of Membrane Transport Proteins and Their Substrate Specificities Using Primary Sequence Information. PLoS ONE, 9(6), e100278.
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Publication 2014
Amino Acid Transporter Anions Biological Processes Carrier Proteins Electrons Gene Products, Protein Membrane Transport Proteins Oligopeptides Proteins RNA, Messenger Staphylococcal Protein A Sugars
2
Validation of Differentially Expressed Genes in Sugarcane
To validate the reliability of differentially expressed genes obtained from Illumina RNA-Seq sequencing, six co-expressed, up-regulated genes from both cultivars: sugar cane_unigene_BMK.40387 (metacaspase-1-like, Q1), sugar cane_unigene_BMK.49302 (ribonuclease 3-like, Q2), sugar cane_unigene_BMK.51436 (pathogenesis-related protein PR-10, Q3), sugar cane_unigene_BMK.57924 (sucrose transporter SUT1, Q4), sugar cane_unigene_BMK.63074 (vacuolar amino acid transporter 1-like, Q5) and sugar cane_unigene_BMK.63784 (heat shock protein-like, Q6) were subjected to RT-qPCR. First-strand cDNAs (10-fold dilution) of sugarcane buds collected from both cultivars 24 h after water inoculation (control) and 24, 48 and 120 h after S. scitamineum inoculation were used as templates, and specific primers were designed according to differential gene sequences [20] (Table S1 in File S1). Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) [21] served as the internal reference gene. SYBR Green staining was applied for RT-qPCR using the ABI 7500 fast real-time PCR system (Applied Biosystems, Foster, CA, USA). The total reaction volume was 25 µL, including 12.5 µL FastStart Universal SYBR Green PCR Master (ROX Medical, Shanghai, China), 0.4 µmol/L primer and 2.0 µL template. Reaction conditions were: 50°C, 2 min; 95°C, 10 min; 95°C, 15 s, 60°C, 1 min, and 40 cycles and three replicates were performed for each. PCR using distilled water as the template was used as a blank control. A 2−ΔΔCt algorithm was applied for quantitative gene expression analysis [22] (link).
Que Y., Su Y., Guo J., Wu Q, & Xu L. (2014). A Global View of Transcriptome Dynamics during Sporisorium scitamineum Challenge in Sugarcane by RNA-seq. PLoS ONE, 9(8), e106476.
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Publication 2014
Adjustment Disorders Amino Acid Transporter DNA, Complementary DROSHA protein, human Gene Expression Profiling Genes Glyceraldehyde-3-Phosphate Dehydrogenases Heat Shock Proteins Membrane Transport Proteins Oligonucleotide Primers pathogenesis Proteins RNA-Seq Saccharum Sucrose SYBR Green I Technique, Dilution Vaccination Vacuole
3
Comprehensive Mining of Rice Amino Acid Transporters
Several approaches were employed for the mining of all putative AAT members in the rice genome. Firstly, BLASTP searches of AAT domains (PF01490 and PF00324) search were performed on website of MSU-RGAP (http://rice. plantbiology. msu.edu/domain_search shtml). Secondly, protein sequences of putative OsAAT members were downloaded from Search Interpro (http://www.ebi.ac.uk/interpro/ISearch?query=PF01490 and PF00324). Thirdly, key words “amino acid transporter” and “amino acid permease” were used as queries to search against Rice Genome Express Database (http://signal.salk.edu/cgi-bin/RiceGE). Resulting protein sequences were then used as queries to perform two database searches against MSU-RGAP (http://rice.plantbiology.msu.edu/) and NCBI (http://www.ncbi.nlm.nih.gov/). After removing the redundant sequences, the remaining protein sequences were submitted to InterProScan (http://www.ebi.ac.uk/Tools/InterProScan/) to confirm the existence of AAT domain. Information about full-length cDNA accessions, coding sequence length, gene structure for each gene and characteristics of proteins were obtained from KOME (Knowledge-based Oryza Molecular biological Encyclopedia) and MSU-RGAP. Gene structures of OsAATs were analyzed on the website of GSDS (Gene Structure Display Server) (http://gsds.cbi.pku.edu.cn/) [65] (link). To predict the putative TM regions in each OsAAT protein, the TMHMM Server v2.0 (http://www.cbs.dtu.dk/services/TMHMM/) was applied with default settings.
Zhao H., Ma H., Yu L., Wang X, & Zhao J. (2012). Genome-Wide Survey and Expression Analysis of Amino Acid Transporter Gene Family in Rice (Oryza sativa L.). PLoS ONE, 7(11), e49210.
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Publication 2012
Amino Acid Permease Amino Acid Sequence Amino Acid Transporter Biopharmaceuticals DNA, Complementary Genes Genetic Structures Genome Open Reading Frames Oryza Oryza sativa Protein Domain rGAP
4
Purification and Identification of Protein Complexes
Cells (1–2×1010) were harvested in log phase, washed in serum-free SDM-79 medium and frozen at −80°C until use. Protein extracts were obtained by resuspending the cell pellet in 1 ml of lysis buffer per 109 cells [10 mM Tris-HCl, pH 7.6, 2 mM DTT, 0.1% (w/v) Igepal CA-630, Complete protease inhibitor cocktail without EDTA (Roche)] and passing the suspension through a 27-gauge syringe thrice on ice. Lysates were centrifuged at 16,000×g for 10 min at 4°C. NaCl was added to the supernatant at a final concentration of 150 mM. TAP procedure was performed as described in [21] (link), except that TEV digestion was carried out overnight at 4°C, and binding to calmodulin beads was allowed to proceed for 4 hours at 4°C. Protein complexes were eluted in 1 ml of 10 mM Tris-HCl, pH 7.4, 150 mM NaCl, 20 mM EGTA, precipitated for 30 min on ice with 20% trichloroacetic acid and 0.08% sodium deoxycholate in siliconized tubes, washed with 100% acetone, air-dried, loaded in 10% PAGE-SDS gels and stained with Sypro Ruby. Protein bands were excised, subjected to MALDI-TOF analysis and identified using MASCOT software (http://www.matrixscience.com).
For RNAses treatment, half of the lysate was incubated with 50 µg of RNase A and 1,000 units of RNase T1 for 30 min on ice before centrifugation. To confirm proper digestion, RNA was extracted from TEV eluate aliquots. cDNA was obtained from 1 µg of DNAse-treated RNA using 0.5 µg of random hexamers (Invitrogen) and Maxima reverse transcriptase (Fermentas), and PCR-amplified using specific primers pairs for the mRNAs encoding the amino acid transporter AATP11 (Tb927.4.4730), the pteridine transporter on chromosome 10, PT-X (Tb927.10.9080), and the nucleobase transporter TbNT10 (Tb927.9.7470), as described [19] (link).
To confirm the association of DRBD3 with different protein partners, small-scale purifications were carried out from 3×109 cells expressing candidate proteins fused to PTP or TAP tags. In this case, TEV eluates were precipitated with trichloroacetic acid as above, loaded in 10% SDS-PAGE gels, transferred to nitrocellulose membranes and assayed for the presence of DRBD3 using anti-DRBD3 antiserum [19] (link).
Fernández-Moya S.M., García-Pérez A., Kramer S., Carrington M, & Estévez A.M. (2012). Alterations in DRBD3 Ribonucleoprotein Complexes in Response to Stress in Trypanosoma brucei. PLoS ONE, 7(11), e48870.
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Publication 2012
Acetone Amino Acid Transporter Buffers Calmodulin Cells Centrifugation Chromosomes, Human, Pair 10 Deoxycholic Acid, Monosodium Salt Deoxyribonucleases Digestion DNA, Complementary Edetic Acid Egtazic Acid Freezing Gels Igepal CA-630 Immune Sera Membrane Transport Proteins Nitrocellulose Oligonucleotide Primers Protease Inhibitors Proteins Pteridines Ribonucleases Ribonuclease T1 RNA, Messenger RNA-Directed DNA Polymerase SDS-PAGE Serum Sodium Chloride Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Sypro Ruby Syringes Tissue, Membrane Trichloroacetic Acid Tromethamine
5
Placental Protein Expression Analysis
Protein expression of total and phosphorylated S6K1 (Thr-389), 4E-BP1 (Thr-37/46 or Thr-70), S6 ribosomal protein (Ser-235/236), Akt (Thr-308), STAT3 (Tyr-705), and AMPKα (Thr-172) was determined in placental homogenates using commercial antibodies (Cell Signaling Technology, Boston, MA). Protein expression of the system A amino acid transporter isoforms (SNAT) 1, 2, and 4 and the system L amino acid transporter isoforms LAT1, LAT2, and 4F2hc was analyzed in placental MVM preparations. The justification for determining protein expression of transporters in MVM rather than in homogenates is that trophoblast nutrient transporters mediate cellular uptake and transfer across the placental barrier only if localized in the syncytiotrophoblast plasma membranes. Thus, data on amino acid transporter protein expression in MVM is much more informative than determination of protein expression in placental homogenates. The SNAT1 antibody was received as a generous gift from Jean Jiang (University of Texas Health Science Center San Antonio). A polyclonal SNAT2 antibody was generated in rabbits (43 (link)). Affinity-purified polyclonal anti-SNAT4 antibodies were produced in rabbits using the epitope YGEVEDELLHAYSKV in human SNAT4 (Eurogentec, Seraing, Belgium). Antibodies targeting the LAT1 and LAT2 were produced in rabbits as described previously (44 (link)). The 4F2hc antibody was purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA), and anti-β actin was from Sigma-Aldrich (St. Louis, MO).
Western blot analysis was performed as previously described (31 (link)). In brief, 20 μg of total protein were loaded onto a SDS-PAGE gel (7% for S6K1, Akt, STAT3, AMPKα, SNAT 1/2/4, and 4F2hc; 12% for 4E-BP1; and 4–12% for LAT1 and LAT2), and electrophoresis was performed at a constant 100 V for 2 h. Proteins were transferred onto nitrocellulose membranes overnight at a constant 30 V. After the transfer, the membranes were blocked in 5% milk in Tris-buffered saline (wt/vol) plus 0.1% Tween 20 (vol/vol) for 1 h at room temperature. Membranes were incubated with primary antibodies overnight at 4 C. Subsequently, membranes were incubated with the appropriate secondary peroxidase-labeled antibodies for 1 h. After washing, bands were visualized using enhanced chemiluminescence detection reagents (GE Healthcare, Chalfont St. Giles, UK). Blots were stripped using β-mercaptoethanol as described previously (45 (link)) and reprobed for β-actin as a loading control. Analysis of the blots was performed by densitometry using an AlphaImager (Alpha Innotech Corp., San Leandro, CA). For each protein target and gestational age, the mean density of the C sample bands was assigned an arbitrary value of 1. Subsequently, all individual C and LP density values at a particular gestational age were expressed relative to this mean.
Rosario F.J., Jansson N., Kanai Y., Prasad P.D., Powell T.L, & Jansson T. (2011). Maternal Protein Restriction in the Rat Inhibits Placental Insulin, mTOR, and STAT3 Signaling and Down-Regulates Placental Amino Acid Transporters. Endocrinology, 152(3), 1119-1129.
Publication 2011
2-Mercaptoethanol Actins Amino Acids Amino Acid Transporter Amino Acid Transport System L Anti-Antibodies Antibodies Carrier Proteins Cells Chemiluminescence Densitometry EIF4EBP1 protein, human Electrophoresis Epitopes Gestational Age Homo sapiens Immunoglobulins Membrane Transport Proteins Milk, Cow's Nitrocellulose Nutrients Oryctolagus cuniculus Peroxidase Placenta Plasma Membrane Protein Isoforms Proteins Protein Targeting, Cellular Ribosomal Proteins Saline Solution SDS-PAGE SLC3A2 protein, human STAT3 protein, human Syncytiotrophoblasts Tissue, Membrane Trophoblast Tween 20 Western Blot

Most recents protocols related to «Amino Acid Transporter»

1
Piglet Jejunal Mucosal RNA Extraction and qRT-PCR Analysis
Total RNA was extracted from the piglet jejunal mucosal samples using the GeneJET RNA Purification Kit (Thermo Fisher Scientific, Waltham, MA, USA) according to the manufacturer’s instructions. DNase treatment was performed to remove contaminating DNA using the TURBO DNA-free™ DNA Removal Kit (Thermo Fisher Scientific, Waltham, MA, USA) following the recommended protocol. The quantity and quality of the RNA were evaluated using a Nanodrop ND 1000 spectrophotometer (Nanodrop Technologies Inc., Wilmington, DE, USA) and agarose gel electrophoresis, respectively. A total of 1000 ng of RNA was then converted into complementary DNA using the High-Capacity RNA-to-cDNA™ Kit (Thermo Fisher Scientific, Waltham, MA, USA) according to the manufacturer’s instructions. Duplex Real Time PCR reactions contained 2 µL cDNA and 8 µL mix containing primers, probe (Additional file 1: Table S1) and 2X TaqMan Mastermix, and were run in triplicate on the Applied Biosystems QuantStudio™ 7 Flex Real-Time PCR system (Thermo Fisher Scientific, Waltham, MA, USA) with the following thermocycler settings: 50 °C for 2 min, 95 °C for 2 min and 40 cycles of 95 °C for 1 s and 60 °C for 20 s. Hydroxymethylbilane synthase (HMBS) was used as housekeeping gene. The following genes were selected and analysed: innate immune signal transduction adaptor (MyD88), nuclear factor kappa B subunit 2 (NFKB2), Occludin (OCLN), Tight junction protein 1 (ZO-1), Mucin 13 cell surface associated (MUC13), glutathione peroxidase 2 (GPX-2), Claudin-4 (CLAUD4), Claudin-3 (CLAUD3), polymeric immunoglobulin receptor (PIGR), branched chain amino acid transaminase 2 (BCAT2), ornithine decarboxylase 1 (ODC1), solute carrier family 6 (neutral amino acid transporter), member 19 (SLC6A19), solute carrier family 7 member 9 (SLC7A9), solute carrier family 1 member 5 (SLC1A5), solute carrier family 38 member 2 (SLC38A2).
QuantStudio Design and Analysis Software v2.5 (Thermo Fisher Scientific, Waltham, MA, USA) was used for determining the gene expression cycle threshold (Ct) values. For each sample the Ct value of the HMBS gene was subtracted from the Ct value of the target gene (ΔCt). The average ΔCt value of the reference animals was then subtracted from the ΔCt value of all the samples (ΔΔCt). The expression of the target gene was given as fold change calculated by 2−ΔΔCt.
Luise D., Correa F., Stefanelli C., Simongiovanni A., Chalvon-Demersay T., Zini M., Fusco L., Bosi P, & Trevisi P. (2023). Productive and physiological implications of top-dress addition of branched-chain amino acids and arginine on lactating sows and offspring. Journal of Animal Science and Biotechnology, 14, 40.
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Publication 2023
Amino Acid Transporter Animals branched chain amino acid aminotransferase Cells Claudin-3 Claudin-4 Deoxyribonuclease I DNA, Complementary Electrophoresis, Agar Gel Family Member Gene Expression Genes Genes, Housekeeping GPX2 protein, human Hydroxymethylbilane Synthase Jejunum Mucins Mucous Membrane NFKB2 protein, human Occludin ODC1 protein, human Oligonucleotide Primers Polymeric Immunoglobulin Receptors Signal Transduction SLC1A5 protein, human SLC6A19 protein, human TJP1 protein, human
2
Transcriptomic Analysis of Mouse Brain
The prefrontal cortex (PFC) and hippocampus (Hipp) of the mouse brain (n=6) were isolated after 7 days of treatment with 4-F-PCP, KET, and SAL. Total RNA was obtained using a Trizol reagent (Invitrogen, Carlsbad, CA, USA). A Hybrid-RTM Kit (GeneAll Biotechnology Co., LTD, Seoul, Korea) was used for further RNA purification. The total RNA concentration was determined with a Colibri Microvolume Spectrometer (Titertek-Berthold, Pforzheim, Germany). The qRT-PCR was utilized to measure the mRNA expression levels of Excitatory amino acid transporters (e.g. EAAT2, EAAT3, EAAT4) and the mTOR. One microgram (ug) of total RNA was reversely transcribed into cDNA using AccuPower CycleScript RT Premix (Bioneer, Seoul, Korea). The cDNA amplification was performed with custom-made sequence-specific primers (Cosmogenetech, Seoul, Korea). The sequences of the primers are provided in the supplementary information (Supplementary Data 2). Relative expression levels were calculated using the 2−ΔΔCt method.
Ortiz D.M., Kim M., Lee H.J., Botanas C.J., Custodio R.J., Sayson L.V., Campomayor N.B., Lee C., Lee Y.S., Cheong J.H, & Kim H.J. (2023). 4-F-PCP, a Novel PCP Analog Ameliorates the Depressive-Like Behavior of Chronic Social Defeat Stress Mice via NMDA Receptor Antagonism. Biomolecules & Therapeutics, 31(2), 227-239.
Publication 2023
Amino Acid Transporter Brain DNA, Complementary FRAP1 protein, human Hybrids Mus Oligonucleotide Primers Prefrontal Cortex RNA, Messenger Seahorses trizol
3
Identifying Sugar Transporter Structures
To obtain the transmembrane domains of these sugar transporters, the amino acid sequences of these sugar transporters were downloaded from the EnsemblFungi database and then submitted to the web server Protter, respectively. To find the ER localization signal motif of sugar transporters, the amino acid sequences of these sugar transporters were submitted to the CLUSTALW online server, and the outcomes were then submitted to the ESPript online server.
Wang H., Pang A.P., Li B., Huo L., Wu F.G, & Lin F. (2023). Intracellular Sugar Transporters Facilitate Cellulase Synthesis in Trichoderma reesei Using Lactose. Biomolecules, 13(2), 295.
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Publication 2023
Amino Acid Transporter Carbohydrate Sequence Membrane Transport Proteins Sugars
4
Evaluating Intestinal Gene Expression in Livestock
Selected mRNA abundance was determined by RT-qPCR, including nutrient transporters genes FABP-1 (fatty acid binding protein 1), FATP-1 (fatty acid transport protein 1), GLUT-2 (glucose transporter 2), LAT-1 (L type amino acid transporter 1), PepT-1 (peptide transporter 1) and SGLT-1 (sodium glucose co-transporter 1), inflammatory molecules’ genes TLR-4 (Toll-like receptor 4), IL-1β (interleukin 1β), IL-8, IL-10, TNF-α (tumor necrosis factor α), TGF-β (Transforming growth factor β) and NF-κB (Nuclear factor kappa B), and tight junction genes Claudin-1, Occludin, ZO-1 and Mucin-2. Total RNA was isolated from ileal mucosa samples (approximately 0.75 mg) using an RNAprep pure tissue kit (Tiangen Biotech Co. Ltd., Beijing, China) under the manufacturer’s instructions. Total RNA concentrations and quality were assessed using a NanoDrop 2000 spectrophotometer (Thermo Fisher Scientific, Waltham, MA, USA). RNA integrity was evaluated using agarose gel (1%) electrophoresis. Then, cDNA was synthesized from 1 μg total RNA using a PrimeScript RT reagent kit (TaKaRa Biotechnology Co., Ltd., Otsu, Japan) following to manufacturer’s protocols. Selected mRNA reactions were detected in 10 μL (Bio-Rad Laboratories, Hercules, CA, USA) using SYBR® Premix Ex TaqTM II (Tli RNaseH Plus) (TaKaRa Biotechnology Co., Otsu, Japan). The primers for nutrient transporters, inflammatory, and tight junction-related and housekeeping genes [glyceraldehyde 3-phosphate dehydrogenase (GAPDH)] were described previously (Wang et al., 2016 (link), 2020 (link)). The 2–ΔΔCt method was used for quantification using GAPDH as a reference gene, and relative abundance was normalized to CON group values.
Han Y., Xu X., Wang J., Cai H., Li D., Zhang H., Yang P, & Meng K. (2023). Dietary Bacillus licheniformis shapes the foregut microbiota, improving nutrient digestibility and intestinal health in broiler chickens. Frontiers in Microbiology, 14, 1113072.
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Publication 2023
1,10-phenanthroline-platinum(II)-ethylenediamine Amino Acid Transporter Claudin-1 DNA, Complementary Electrophoresis FABP1 protein, human Fatty Acid Transport Proteins Genes Genes, Housekeeping Glyceraldehyde-3-Phosphate Dehydrogenases IL1B protein, human IL10 protein, human Ileum Inflammation Membrane Transport Proteins Mucin-2 Mucous Membrane NF-kappa B Nutrients Occludin Oligonucleotide Primers Peptide Transporter 1 RELA protein, human RNA, Messenger Sepharose SLC2A2 protein, human Sodium-Glucose Transporter 1 Tight Junctions Tissues TLR4 protein, human TNF protein, human Transforming Growth Factor beta Transforming Growth Factors Tumor Necrosis Factor-alpha
5
Immunofluorescence Analysis of Mammary Gland Tissues
Immunofluorescence analyses were performed using the reported methods [26 (link), 27 (link)]. The mammary gland tissues were fixed, dehydrated, and embedded in paraffin. Sections of the tissues (3 μm thick) were then air-dried on MAS-coated slides. After deparaffinization, antigen retrieval was performed by autoclaving the sections in a citric acid buffer (pH 6.0) for 20 min at 121 °C. Cultured GMECs on collagen gel isolated from the insert were fixed with methanol for 10 min at − 20 °C and then with 1% paraformaldehyde in PBS for 10 min at 4 °C. Subsequently, the tissue sections and cells were washed with PBS for 10 min, after which they were incubated in PBS-T (PBS containing 0.05% Tween-20) containing 5% bovine serum albumin (MP Biomedicals) for 1.5 h at room temperature. The sections and cells were then incubated overnight at 4 °C with rabbit polyclonal antibodies against L-amino acid transporter (LAT)-1 (#ab208776; Abcam, Cambridge, UK, 1:100), LAT3 (#ab254719; Abcam, 1:100), and claudin 3 (#34-1700, Thermo Fisher Scientific, 1:200) or with mouse monoclonal antibodies against occludin (#sc-133,256; Santa Cruz Biotechnology, 1:200) diluted in PBS-T containing 2.5% bovine serum albumin. To evaluate immunofluorescence, the sections and cells were incubated with secondary antibodies (Alexa Fluor 488–conjugated goat anti-rabbit, #A32731, 1:400; Alexa Fluor 555–conjugated goat anti-mouse, #A32727, 1:400; both Thermo Fisher Scientific) diluted with PBS-T containing 2.5% bovine serum albumin for 1 h at room temperature. Immunofluorescence images were obtained using a fluorescence microscope (BZ-9000) and processed using analysis software (Keyence, Osaka, Japan).
Tsugami Y., Nii T, & Isobe N. (2023). Valine Treatment Enhances Antimicrobial Component Production in Mammary Epithelial Cells and the Milk of Lactating Goats Without Influencing the Tight Junction Barrier. Journal of Mammary Gland Biology and Neoplasia, 28(1), 3.
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Publication 2023
alexa fluor 488 Alexa Fluor 555 Amino Acid Transporter Antibodies Antigens Buffers Cells Citric Acid Claudin-3 Collagen Fluorescent Antibody Technique Goat Mammary Gland Methanol Microscopy, Fluorescence Monoclonal Antibodies Mus Occludin Paraffin Embedding paraform Rabbits Serum Albumin, Bovine SLC43A1 protein, human Tissues Tween 20

Top products related to «Amino Acid Transporter»

1
Trizol reagent by Thermo Fisher Scientific
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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
2
Proton coupled amino acid transporter pat2 by Santa Cruz Biotechnology
Sourced in Germany, United Kingdom
The Proton-coupled amino acid transporter (PAT2) is a laboratory equipment that facilitates the transport of amino acids across cell membranes. It functions by coupling the movement of amino acids to the electrochemical gradient of protons, allowing for the efficient uptake and distribution of these essential biomolecules.
3
β actin by Santa Cruz Biotechnology
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β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is a component of the microfilament system and plays a crucial role in various cellular processes, such as cell motility, maintenance of cell shape, and intracellular trafficking.
4
Dl tboa by Bio-Techne
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DL-TBOA is a potent and selective excitatory amino acid transporter (EAAT) inhibitor. It acts as an antagonist for EAAT1 and EAAT2. DL-TBOA is used in research applications to study the function and regulation of glutamate transport systems.
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4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific
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LAMP2 is a lysosome-associated membrane glycoprotein that plays a role in the fusion of lysosomes with autophagosomes during the process of autophagy. It is commonly used as a marker for autophagic structures.
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FOXO1 is a protein that plays a crucial role in the regulation of cellular processes such as cell cycle progression, apoptosis, and metabolism. It functions as a transcription factor, binding to specific DNA sequences and modulating the expression of target genes. FOXO1 is involved in diverse biological pathways and its activity is regulated by various post-translational modifications and signaling cascades.
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Ampkα by Cell Signaling Technology
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AMPKα is a catalytic subunit of the AMP-activated protein kinase (AMPK) complex. AMPK is a cellular energy sensor that plays a crucial role in maintaining energy homeostasis within cells. AMPKα is responsible for the phosphorylation and activation of AMPK, which then regulates various metabolic pathways in response to changes in cellular energy levels.
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Pico tag reverse phase column by Waters Corporation
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The PICO-TAG reverse-phase column is a high-performance liquid chromatography (HPLC) column designed for the separation and analysis of amino acid derivatives. It features a silica-based packing material with a proprietary surface chemistry for efficient and selective separation of a wide range of amino acid derivatives.
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Rneasy mini kit by Qiagen
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.

More about "Amino Acid Transporter"

Amino acid transporters, also known as membrane transport proteins or nutrient transporters, are a crucial component of cellular metabolism and signaling pathways.
These transmembrane proteins facilitate the movement of amino acids, the building blocks of proteins, across biological membranes.
The TRIzol reagent, a popular RNA extraction method, can be used to isolate and study the expression of genes encoding amino acid transporters.
The Proton-coupled Amino Acid Transporter (PAT2) is a specific type of amino acid transporter that plays a role in nutrient uptake and cellular signaling. β-actin, a commonly used housekeeping gene, can be employed as a reference to normalize the expression of amino acid transporter genes.
DL-TBOA, a specific inhibitor of amino acid transporters, can be utilized to investigate their functional roles.
DAPI, a fluorescent dye, can be used to visualize cellular nuclei, while LAMP2 antibodies can help identify lysosomal compartments in which amino acid transporters may reside.
Transcription factors like FOXO1 and signaling kinases such as AMPKα have been shown to regulate the expression and activity of amino acid transporters, highlighting their importance in cellular homeostasis and metabolic processes.
The PICO-TAG reverse-phase column can be used for the separation and quantification of amino acids, including those transported by these membrane proteins.
For comprehensive analysis of amino acid transporter expression and function, researchers can leverage the RNeasy Mini Kit for RNA isolation and qRT-PCR techniques.
PubCompare.ai, the leading AI-driven platform, can optimize your amino acid transporter research by providing access to relevant protocols, pre-prints, and patents, as well as AI-driven comparisons to identify the best experimental approaches and products.
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