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AQP1 protein, human

AQP1 (aquaporin-1) is a water-channel protein that facilitates the transport of water across cell membranes.
It plays a crucial role in maintaining fluid balance and homeostasis within the body.
AQP1 is expressed in various tissues, including the kidney, red blood cells, and the central nervous system.
Researchers studying AQP1 can optimize their investigations with PubCompare.ai, an AI-driven platform that enhances reproducibility and accuracy.
This tool helps scientists easily locate the best protocols from literature, preprints, and patents using AI-powered comparisons, streamlining the research process and identifying the most reliable products to support AQP1 studeis.

Most cited protocols related to «AQP1 protein, human»

The detailed methods are described in the Supporting Information. In summary, we embedded 10 membrane proteins in
a previously characterized model of the plasma membrane.20 (link) The starting structures of the 10 membrane proteins
simulated in this study were taken from the Protein Data Bank or obtained
from the corresponding publication: aquaporin-1 (AQP1, PDB ID 1J4N);98 (link) prostaglandin H2 synthase (COX1, PDB ID 1Q4G);99 (link) the dopamine transporter (DAT, PDB ID 4M48);44 (link) the epidermal growth factor receptor (EGFR);77 (link) AMPA-sensitive glutamate receptor 2 (GluA2,
PDB ID 3KG2);100 (link) glucose transporter 1 (GluT1, PDB ID 4PYP);101 (link) voltage-dependent Shaker potassium channel 1.2 (Kv1.2,
PDB ID 3LUT,102 (link) residues 32 to 4421 for each monomer); sodium,
potassium pump (Na,K-ATPase, PDB ID 4HYT);103 (link) δ-opioid
receptor (δ-OPR, PDB ID 4N6H);104 (link) and P-glycoprotein
(P-gp, PDB ID 4M1M).105 (link) In each system, four copies of each
protein were included and positioned at a distance of ca. 20 nm from
each other. Proteins were simulated using standard Martini protocols
with minor variations between systems to accommodate system-specific
issues (Supporting Information). The following
lipid classes were included: cholesterol (CHOL), in both leaflets;
charged lipids phosphatidylserine (PS), phosphatidic acid (PA), phosphatidylinositol
(PI), and the PI-phosphate, PI-bisphosphate, and PI-trisphosphate
(PIPs) placed in the inner leaflet; and ganglioside (GM) in the outer
leaflet. The zwitterionic phosphatidylcholine (PC), phosphatidylethanolamine
(PE), and sphingomyelin (SM) lipids were placed in both leaflets,
with PC and SM primarily in the outer leaflet and PE in the inner
leaflet. Ceramide (CER), diacylglycerol (DAG), and lysophosphatidylcholine
(LPC) lipids were also included, with all the LPC in the inner leaflet,
and CER and DAG primarily in the outer leaflet. The details of the
Martini lipids used in this study can be found on the Martini Lipidome
webpage (http://www.cgmartini.nl/index.php/force-field-parameters/lipids) and are described by Ingolfsson et al., and Wassenaar et al.20 (link),106 (link) The exact lipid composition of each system is given in the Supporting Information. The systems are ca. 42
× 42 nm in the membrane plane (x and y), including 4 proteins and ca. 6000 lipids.
Production
runs were performed in the presence of weak position
restraints applied to the protein backbone beads, with a force constant
of 1 kJ mol–1 nm–2, preventing
proteins from associating with each other. Each of the systems has
been simulated for 30 μs, which turned out to be adequate to
obtain convergence of major lipid components in the lipid shells around
the individual copies of the proteins (Supporting Information). Additional control simulations were performed
in the AQP1 system, in order to test the effects of simulation length,
position restraints on the proteins, lipid composition, and water
model on the results of lipid composition near the proteins (Supporting Information).
Simulations were
performed using the GROMACS simulation package
version 4.6.3,107 (link) with the Martini v2.2
force field parameters,62 (link),63 (link) and standard simulation
settings.108 (link) Additional details are provided
in Supporting Information. All the analyses
were performed on the last 5 μs of each simulation system.
Publication 2018
Adenosinetriphosphatase alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid AMPA Receptors AQP1 protein, human Aquaporin 1 Cell Membrane Proteins Ceramides Cholesterol Debility Diacylglycerol Dopamine Transporter Epidermal Growth Factor Receptor Gangliosides Glucose Transporter Glutamate Glutamate Receptor Lipids Lysophosphatidylcholines Na(+)-K(+)-Exchanging ATPase P-Glycoproteins Phosphates Phosphatidic Acid Phosphatidylcholines phosphatidylethanolamine Phosphatidylinositols Phosphatidylserines Potassium Channel Proteins PTGS1 protein, human SLC2A1 protein, human Sphingomyelins Tissue, Membrane Vertebral Column

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Publication 2009
AQP1 protein, human Biological Assay Cell Adhesion Cells Cloning Vectors E-Cadherin Erythrocytes Fluorescence Glutaral L Cells Microscopy Proteins Serum
This study was approved by our Institutional Animal Care Committee. Fifteen CBA/CaJ mice ranging in age from 4 weeks to 12 weeks were deeply anesthetized and intracardially perfused with one of 3 fixatives, 4% formaldehyde (F), 4% formaldehyde + 1% acetic acid (FA), and 4% formaldehyde + 1% acetic acid + 0.1% glutaraldehyde (FGA). The temporal bones were removed and fixed for an additional 25 hours at room temperature. Decalcification was accomplished using 120 mM ethylenediaminetetraacetic acid at a pH of 7 for seven days. The temporal bones were rinsed in distilled water and dehydrated in ethanols. In nine of the fifteen mice, the left ears were embedded in polyester wax (Electron Microscopy Sciences, Fort Washington, PA) and the right ears were embedded in celloidin (parlodion strips) (Mallinckrodt Chemicals, Phillipsburg, NJ). Both ears of the remaining six mice were embedded in paraffin (Paraplast X-TRA) (McCormick Scientific, St. Louis, MO). Temporal bones were sectioned at a thickness of 8-20 μm depending on the embedding medium. Paraffin sections were sectioned at 8 μm thickness and mounted on superfrost plus slides. Polyester wax sections were sectioned at 10 μm and mounted on superfrost slides coated with 0.5% bovine albumin and 0.5% fish gelatin [Merchant et al., 2006 (link)]. Celloidin sections were sectioned at 20 μm and those being immunostained were mounted on subbed glass slides smeared with albumin and fixed in place with formalin-soaked bibulous paper. A wooden block was placed on top of the bibulous paper and a 500g weight was placed on the block. The sections were dried for 1 hour under the weight.
Every tenth section was stained with hematoxylin and eosin and examined by light microscopy. Preservation of morphology within the scala media of the cochlea was assessed for each of the three fixatives and each of the three embedding media.
Prior to immunostaining, selected paraffin sections were dewaxed using xylenes, polyester wax was removed using ethyl alcohols [Merchant et al., 2006 (link)], and celloidin was removed using a solution of sodium hydroxide mixed in methanol [Miguel-Hidalgo and Rajkowska, 1999 (link)]. The sodium hydroxide methanol (NaOH-methanol) solution was made in the same manner as that described by Miguel-Hidalgo and Rajkowska; however the subsequent steps were modified. Once mixed, the solution was diluted 1:2 with methanol instead of 1:3 and used immediately. The amount of time the sections were exposed to the NaOH-Methanol solution was reduced from 30 minutes to 15 minutes (3 × 5 minutes) with 100% methanol rinses between each 5 minute change. The 3% H2O2step described by Miguel-Hidalgo and Rajkowska was omitted. The sections were hydrated from 100% methanol (10 minutes), through 70% methanol (10 minutes), and into distilled water. Following hydration, the sections were rinsed in 0.01 M phosphate buffered saline (PBS, pH 7.3), incubated in 5% normal horse serum for one hour, then incubated in primary antibodies overnight at room temperature in a humid chamber.
Immunostaining was accomplished using antibodies to prostaglandin d synthase (PGDS, Caymen) at a dilution of 1:5000, aquaporin 1 (Aqp1, Chemicon) at a dilution of 1:1000, connective tissue growth factor (CTGF, Cell Sciences) at a dilution of 1:10,000, 200 kD neurofilament (NF, Boehringer Mannheim) at a dilution of 1:2000, tubulin (Sigma) at a dilution of 1:15,000, and Na+,K+-ATPase (Siegel) at a dilution of 1:10,000. Following 14 hour primary antibody incubations, sections were rinsed in three washes of PBS. Secondary antibodies appropriate for the host species of primaries, at a dilution of 1:200, were applied and incubated for 1 hour. Following another three rinses in PBS, avidin-biotin-horseradish peroxidase (Standard ABC Kit, Vector Labs, Burlingame, CA) was applied to the sections and left to incubate for 1 hour, followed again by three washes with PBS. Finally, the sections were colorized using 0.01% diaminobenzidine and 0.01% H2O2 for between 5 and 10 minutes, rinsed, dehydrated, and cover slips were applied. Immunostaining was repeated at least once with each antibody, and in most cases, multiple times. The immunostained sections were analyzed by light microscopy and given a rating of no staining (−), adequate staining (+), good staining (+ +), or very good staining (+ + +).
Publication 2008
Acetic Acid Adenosine Triphosphatases Albumins Animal Care Committees Antibodies AQP1 protein, human Aquaporin 1 Avidin Biologic Preservation Biotin Celloidin Cells Cloning Vectors Cochlea Connective Tissue Growth Factor Duct, Cochlear Ear Edetic Acid Electron Microscopy Eosin Equus caballus Ethanol Fishes Fixatives Formaldehyde Formalin Gelatins Glutaral Horseradish Peroxidase Host Specificity Immunoglobulins Light Microscopy Methanol Mice, Inbred CBA Mus Neurofilaments Paraffin Paraffin Embedding Peroxide, Hydrogen Phosphates Polyesters prostaglandin R2 D-isomerase Prostaglandins D Saline Solution Serum Serum Albumin, Bovine Sodium Hydroxide Technique, Dilution Temporal Bone Tubulin Xylenes
Mouse kidney and small intestine were fixed with 4% paraformaldehyde, and were subsequently immersed in 30% (w/v) sucrose. Samples were blocked in PBS containing 5.0% (v/v) BSA after slides were made with a cryostat, and were subsequently incubated with our anti-KSP antibody, anti-AQP1 antibody (Santa Cruz), anti-Megalin antibody kindly provided by Dr. Sekine (Tokyo Metropolitan Institute of Medical Science, Japan) [17] (link), anti-E-cadherin antibody (Abcam) and anti-AQP2 antibody (Sigma). Alexa Fluor 488 and 594 (Invitrogen) were used as a second antibody. Nuclei were stained with DAPI (Invitrogen). Pictures were taken with TCS-SP5 (Leica) and Olympus IX81.
Mouse ES cells were stained at day 18 of the differentiation with Activin (10 ng/mL) after fixation with 4% paraformaldehyde. The samples were blocked in PBS containing 5.0% BSA and were incubated with our anti-KSP antibody conjugated with biotin and anti-E-cadherin antibody (Cell Signaling). Streptoavidin-Cy5 (Beckman Coulter) and Alexa Fluor 594 (Invitrogen) were used for the detection of KSP and E-cadherin respectively.
KSP-positive and KSP-negative cells were stained on the day after the flow cytometry. The samples were treated with Endogenous Avidin/Biotin Blocking System (Abcam) and were subsequently blocked in PBS containing 5.0% BSA and 0.1% Triton. The samples were incubated with our anti-KSP antibody conjugated with biotin, anti-human specific mitochondria antibody conjugated with biotin (Abcam), anti-Megalin antibody, anti-AQP2 (Alomone Labs) or anti-Podocalyxin (R&D) antibodies. Streptavidin-Phycoerythrin (Beckman Coulter) or Alexa Fluor 594 was used for detection.
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Publication 2013
Activins Alexa594 alexa fluor 488 Antibodies Antibodies, Anti-Idiotypic AQP1 protein, human Avidin Biotin Cadherins CDH1 protein, human Cell Nucleus Cells DAPI Embryonic Stem Cells Flow Cytometry Homo sapiens Immunoglobulins Intestines, Small Kidney LDL-Receptor Related Protein 2 Mitochondria Mus paraform Phycoerythrin podocalyxin Streptavidin Sucrose

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Publication 2012
Acetone Adenocarcinoma, Clear Cell anti-IgG AQP1 protein, human Biological Markers Buffers Cancer of Kidney Cardiac Arrest Common Cold Creatinine Equus asinus Gels Immunoglobulins link protein Methanol Patients Proteins Rabbits Sulfate, Sodium Dodecyl Technique, Dilution Tissue, Membrane Tween 20 Urine Western Blot Western Blotting

Most recents protocols related to «AQP1 protein, human»

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Example 2

The specificity of the compounds is tested against the most closely related of the 13 known aquaporins: AQP1, AQP2, AQP5 and both splice variants of AQP4 (A and B). A stable CHO cell line is created for each of the above aquaporins and the inhibition of water permeability using the Aquaporin-Mediated Cell Volume Change Assay with 10 μM Compound 3 is tested. Compound 3 inhibits AQP2 and 4, while it poorly inhibits AQP1 and 5 (FIG. 2).

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Patent 2024
AQP1 protein, human Aquaporin 2 Aquaporin 3 Biological Assay Cardiac Arrest Cell Lines Permeability Psychological Inhibition Water Channel
H&E staining of 4-μm-thick formalin-fixed, paraffin embedded kidney tissue sections was performed according to standard protocols. Images were captured by microscopy (Olympus BX53). In each kidney, the numbers of damaged tubules were counted separately in 10 nonoverlapping fields observed at ×400 magnification. Renal tubular injury scores expressed as the percentage of damaged tubules, and the mean values were calculated (GraphPad Prism). For immunofluorescence staining of kidney tissue sections, heat-induced antigen retrieval was performed by heating sections in 1 mM EDTA at 95 °C in a pressure cooker for 20 min and then 20 min of cooling at room temperature. Sections were permeabilized with 0.1% Triton X-100 in 1× PBS. Sections were incubated for 30 min at room temperature with blocking buffer 5% BSA in 1× PBS and subsequently incubated with primary antibodies including anti-dsRNA mAb J2, anti-PNPT1, anti-AQP1, and anti-podocin antibodies for 3 h. Sections were washed in 1× PBS three times and then incubated with secondary antibodies including goat anti-mouse Alexa Fluor 488, donkey anti-rabbit Alexa Fluor594, donkey anti-rabbit Alexa Fluor 488, and goat anti-mouse Alexa Fluor 594 antibodies for 1 h at room temperature followed by 3 washes with 1× PBS. The sections were then mounted in Prolong Diamond Antifade Mountant with DAPI. Confocal images were taken using a confocal microscope (Zeiss LSM 880) with ZEN 3.1 blue edition software. Fluorescence intensities were quantified using ImageJ 1.44p software.
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Publication 2023
Alexa594 alexa fluor 488 Anti-Antibodies Antibodies Antigens AQP1 protein, human Buffers DAPI Diamond Edetic Acid Equus asinus Fluorescence Fluorescent Antibody Technique Formalin Goat Injuries Kidney Microscopy Microscopy, Confocal Mus NPHS2 protein Paraffin Embedding PNPT1 protein, human Pressure prisma Rabbits RNA, Double-Stranded Tissues Triton X-100 Tubule, Kidney
HK2 cells were obtained from American Tissue and Cell Center (ATCC, CRL-2190) and grown as a monolayer in DMEM/F12 (Gibco) supplemented with 10% FBS (Gibco), 100 U/ml penicillin (Gibco), 100 μg/ml streptomycin (Gibco) and ITS (Sigma-Aldrich). Primary antibodies for dsRNA mAb J2 (Scions, 10010500, 1:200), PNPT1 (Abcam, ab96176, 1:200/2000), AQP1 (Abcam, 168387, 1:200), synaptopodin (Abcam, ab224491, 1:100), podocin (Sigma-Aldrich, P0372, 1:100), PKR (Abcam, ab32506, 1:1000), p-PKR (Abcam, ab32036, 1:1000), eIF2α (CST, 5324 S, 1:1000), p-eIF2α (CST, 3398 S, 1:1000), ATF4 (Abcam, ab184909), COX IV (Abcam, ab14744, 1:1000), LaminB1 (Abcam, ab65986, 1:1000), and α-tubulin (Proteintech, 11224-1-AP, 1:2000) were used for immunofluorescence and western blot analysis; Secondary antibodies including goat anti-mouse Alexa Fluor 488 (Invitrogen, A11001, 1:1000), donkey anti-rabbit Alexa Fluor 594 (Invitrogen, A21207, 1:1000), donkey anti-rabbit Alexa Fluor 488 (Invitrogen, A21206, 1:1000), goat anti-mouse Alexa Fluor 594 (Invitrogen, A11005, 1:1000), goat anti-mouse IgG-HRP (Santa Cruz Biotechnology, sc-2005, 1:1000) and goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology, sc-2004, 1:1000) were used correspondingly. DAPI was purchased from Santa Cruz Biotechnology (sc-3598, 1:1000). TGFβ (R&D Systems, 7754), LPS (Sigma-Aldrich, L2630), HG (Sigma-Aldrich, G7021) were used. Digitonin (Sigma-Aldrich, D141) were used for membrane permeabilization. KIM-1 (Abcam, ab213477), NGAL (Abcam, ab118901), β2-MG (Abcam, ab223590) ELISA quantitation kits, creatinine kit (Sigma-Aldrich, MAK080), calcium assay kit (Sigma-Aldrich, MAK022) and phosphorus microplate assay kit (Absin, 580107) were purchased for renal tubular injury assessment. Lipofectamine RNAi MAX (Invitrogen, 13778150) were used for transfection. PKR inhibitor (C16) was obtained from Sigma-Aldrich (I9785) and dissolved in DMSO prior to experiment. IMT1 was obtained from MCE (HY-134539) and dissolved in DMSO prior to experiment. FITC-Annexin V Apoptosis Detection Kit (Invitrogen, V13241) and TUNEL Bright-Green apoptosis detection kit (Vazyme, A112) were used for apoptosis analysis. Collagenase D (1 mg/mL, C6885), protease (1 mg/mL, P6911) and DNaseI (1 U/mL, D5025) were purchased from Sigma-Aldrich. Click-iT® Plus OPP Protein Synthesis Assay Kits were purchased from Life Technologies (C10456). PierceTM Classic IP Kit were purchased from Thermo Fisher Scientific (26146). RiboTM Fluorescent In Situ Hybridization Kit were purchased from Ribo (C10910). PNPT1 AAV were purchased from OBiO (H131559). siPNPT1 plasmid (siG000087178A-1-5) and siPKR plasmid (siB161220105622-1-5) were purchased from Ribo.
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Publication 2023
Alexa594 alexa fluor 488 alpha-Tubulin Annexin A5 anti-IgG Antibodies Apoptosis AQP1 protein, human ATF4 protein, human Biological Assay Calcium Cells collagenase 1 Creatinine DAPI Digitonin Enzyme-Linked Immunosorbent Assay Equus asinus Fluorescein-5-isothiocyanate Fluorescent in Situ Hybridization Goat HAVCR1 protein, human Immunofluorescence Injuries In Situ Nick-End Labeling LCN2 protein, human Lipofectamine Mus NPHS2 protein Penicillins Peptide Hydrolases Phosphorus Plasmids PNPT1 protein, human Protein Biosynthesis Rabbits RNA, Double-Stranded RNA Interference Streptomycin Sulfoxide, Dimethyl SYNPO protein, human Tissue, Membrane Tissues Transfection Transforming Growth Factor beta Tubule, Kidney Western Blot
Ten mice were bred from a C57BL/6 background (5 WT AQP1+/+, 4 KO AQP1−/− and 1 HT AQP1−/+) and the intestines provided by from the Department of Physiology of the Hannover Medical School (Hannover, Germany). The AQP1-KO mice had been generated from breeding pairs of heterozygous AQP−/+ mice kindly provided by Dr. Alan S. Verkman (San Francisco, CA, USA; Ma et al., 1998). Animals were anaesthetized and sacrificed in accordance with the German Tierschutzgesetz §4 2015/222. Organs, specifically the esophagus, stomach, duodenum, jejunum, ileum, cecum, and colon were immediately removed. These organs were separately snap frozen and cryo-conserved. Each organ was embedded in OCT (TissueTek; Thermofisher Scientific Inc., Waltham, MA, USA) according to a modification of the “Swiss role” described by Meier-Ruge [65 ], with exception of the esophagus, which was embedded as a tube for cryo-cutting. The samples were cut with the cryotome (Leica CM1950) into 7 µm slices, fixed on a microscope slide and stored at minus 20 °C.
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Publication 2023
Animals AQP1 protein, human Cecum Colon Duodenum Esophagus Freezing Heterozygote Ileum Intestines Jejunum Mice, Laboratory Microscopy physiology Stomach
The slices were stained by routine H.E. staining as well as immunohistochemically stained for AQP1 with the Cell and Tissue staining Rabbit Kit HRP-AEC System (R&D Systems, Minneapolis, MN, USA). The kit was used according to the R&D System’s protocol, and a rabbit primary antibody against AQP1 (Sigma-Aldrich, Merck, Millipore, Burlington, MA, USA) was used at a dilution of 1:400. The samples were than counterstained with hematoxylin (Spitalpharmazie USB, Basel, Switzerland), mounted with aquatex (Merck KGaA, Darmstadt, Germany) and covered up with a Cover-Slip. Every staining was accompanied with a negative control using antibody diluent (DAKO, Glostrup, Denmark).
Immunofluorescence staining was performed as a triple staining with antibodies against AQP1, calretinin, and S100B. The staining was performed according to a standardized protocol, using the rabbit anti-AQP1 antibody (Merck Millipore, Darmstadt, Germany) at a dilution of 1:400, the chicken anti-calretinin antibody (Synaptic Systems, Göttingen, Germany) at a dilution of 1:200 and the guinea pig anti-S100B antibody (Synaptic Systems, Göttingen, Germany) at a dilution of 1:400. As secondary antibodies, anti-rabbit A488 (Invitrogen, Carlsbad, CA, USA), anti-chicken A647 (Invitrogen, Carlsbad, CA, USA), and anti-guinea pig A555 (Invitrogen, Carlsbad, CA, USA) were used at a dilution of 1:2000. Tissue slices were mounted with DAPI (Life Technologies, Thermo Fischer Scientific Inc., Waltham, MA, USA). For every sample an additional negative control without the primary antibodies, was carried out.
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Publication 2023
Antibodies Antibodies, Anti-Idiotypic AQP1 protein, human Calretinin Cavia Cells Chickens Cover-up DAPI Fluorescent Antibody Technique Hematoxylin Immunoglobulins Rabbits Technique, Dilution Tissues

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More about "AQP1 protein, human"

Aquaporin-1 (AQP1) is a crucial water-channel protein that facilitates the transport of water across cell membranes.
This integral membrane protein plays a vital role in maintaining fluid balance and homeostasis within the human body.
AQP1 is widely expressed in various tissues, including the kidney, red blood cells, and the central nervous system.
Researchers studying AQP1 can optimize their investigations by utilizing PubCompare.ai, an innovative AI-driven platform that enhances reproducibility and accuracy in research.
This powerful tool helps scientists easily locate the best protocols from literature, preprints, and patents through AI-powered comparisons, streamlining the research process and identifying the most reliable products to support AQP1 studies.
When investigating AQP1, researchers may also consider using other key reagents and tools, such as TRIzol reagent for RNA extraction, Lipofectamine 2000 for transfection, and the RNeasy Mini Kit for purifying high-quality RNA.
Additionally, antibodies like Ab168387 and Ab15080 can be employed for detecting and quantifying AQP1 expression.
PVDF membranes are commonly used for Western blotting to analyze AQP1 protein levels, while FBS and DAPI can be utilized in cell culture and immunofluorescence experiments, respectively.
By leveraging these resources and technologies, researchers can enhance their understanding of AQP1 and its critical functions within the human body, paving the way for advancements in various fields, such as nephrology, neuroscience, and hematology.
Teh PubCompare.ai platform is a valuable tool that can streamline the research process and lead to more reliable and reproducible findings.