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Sodium thiosulfate
Sodium thiosulfate
Sodium thiosulfate is a versatile chemical compound with a wide range of applications in research and industry.
It is commonly used as a reducing agent, a fixing agent in photography, and a treatment for certain medical conditions.
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It is commonly used as a reducing agent, a fixing agent in photography, and a treatment for certain medical conditions.
PubCompare.ai's AI-driven platform allows researchers to discover the power of sodium thiosulfate by locating the best research protocols from literature, pre-prints, and patents through comprehensive search.
Users can optimize their workflow with AI-driven comparisons that help identify the most effective protocols and products, experieancing the future of research today.
Most cited protocols related to «Sodium thiosulfate»
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Animals and treatment: Adult male Sprague–Dawley rats (225–250 g,
n=36) were purchased from Samtako Animal Breeding Center (Osan, Korea)
and were randomly divided into a sham-operated group, vehicle-treated group and
resveratrol-treated group (n=12 per group). All procedures for animal use
were approved by the Institutional Animal Care and Use Committee of Gyeongsang National
University (GNU-130723-R0050). Experimental animals were housed at 18–22°C under a 12 hr
light/12 hr dark cycle and had free access to a pellet diet and tap water. Resveratrol (30
mg/kg, Sigma, St. Louis, MO, U.S.A.) was dissolved in 2% dimethyl sulfoxide (DMSO) as
vehicle and was injected intraperitoneally as described previously [19 (link)]. Resveratrol or vehicle was
injected immediately after middle cerebral artery occlusion (MCAO).
Middle cerebral artery occlusion: Rats were anesthetized with sodium
pentobarbital (100 mg/kg), and MCAO was carried out as described previously [21 (link)]. Briefly, the right common
carotid artery, external carotid and internal carotid were exposed through a midline cut. A
4/0 nylon filament with a heated rounded tip was inserted from the external carotid artery
into the internal carotid artery and advanced until the rounded tip occluded the origin of
the middle cerebral artery. Sham-operated animals were subjected to the same procedure,
except for insertion of the filament. At 24 hr after the onset of permanent occlusion,
animals were decapitated, and the right cerebral cortex was isolated.
2-Dimensional gel electrophoresis: Proteomic analysis was carried out as
our previously described method [32 (link)].
Proteins were extracted from the right cerebral cortex by homogenization in buffer solution
(8 M urea, 4% CHAPS, ampholytes and 40 mM Tris–HCl) followed by centrifugation at 16,000 g.
Protein concentration was determined by the Bradford method (Bio-Rad, Hercules, CA, U.S.A.)
according to the manufacturer’s protocol. Immobilized pH gradients (IPG, pH 4–7 and pH 6–9,
17 cm, Bio-Rad) were incubated in rehydration buffer (8 M urea, 2% CHAPS, 20 mM DTT, 0.5%
IPG buffer and bromophenol blue) for 13 hr at room temperature. Assayed protein samples were
loaded on IPG strips (pH 4–7 and 6–9), and isoelectric focusing (IEF) was performed as
follows: 200 V (1 hr), 500 V (1 hr), 1,000 V to 8,000 V (30 min) and 8,000 V (5 hr) using an
IPG phore unit (GE Healthcare, Uppsala, Sweden). Strips were incubated with equilibration
buffer (6 M urea, 30% glycerol, 2% sodium dodecyl sulfate, 50 mM Tris-HCl and bromophenol
blue) and loaded on gradient gels (7.5–17.5%), followed by second-dimension electrophoresis
using Protein-II XI electrophoresis equipment (Bio-Rad). Settings were 5 mA per gel for 2 hr
followed by 10 mA per gel at 10°C.
Silver staining, image analysis and protein identification: Silver
staining was performed as follows: fixation (12% acetic acid and 50% methanol) for 2 hr,
washing with 50% ethanol and then treatment with 0.2% sodium thiosulfate. Gels were washed
with deionized water and stained in silver solution (0.2% silver nitrate). Gels were
developed in 0.2% sodium carbonate solution, and gel images were collected using an Agfar
ARCUS 1200™ scanner (Agfar-Gevaert, Mortsel, Belgium). PDQuest 2-D analysis software
(Bio-Rad) was used to analyze differences in protein spots among the different groups.
Differentially expressed protein spots were excised and destained. Gel particles were
digested in trypsin-containing buffer, and the extracted peptides were analyzed using a
Voyager-DETM STR biospectrometry workstation (Applied Biosystem, Forster City, CA, U.S.A.)
for peptide mass fingerprinting. Database searches were carried out using MS-Fit and
ProFound software. SWISS-PROT and NCBI were used as protein sequence databases.
Western blot analysis: Western blot analysis was carried out as our
previously described method [13 (link),
32 (link)]. Right cerebral cortex was dissolved in lysis
buffer (1 M Tris–HCl, 5 M sodium chloride, 0.5% sodium deoxycholate, 10% sodium dodecyl
sulfate, 1% sodium azide and 10% NP-40). Protein concentration was determined using a
bicinchoninic acid (BCA) kit (Pierce, Rockford, IL, U.S.A.) according to the manufacturer’s
protocol. Equal volumes of protein (30 µg per sample) were electrophoresed
on 10% SDS-PAGE gels, and the proteins were transferred to poly-vinylidene fluoride (PVDF)
membranes (Millipore, Billerica, MA, U.S.A.). To minimize nonspecific binding, membranes
were blocked with skim milk for 1 hr at room temperature. PVDF membranes were washed in
Tris-buffered saline containing 0.1% Tween-20 (TBST) and then incubated with antibodies
against the following proteins: peroxiredoxin-5, isocitrate dehydrogenase [NAD+],
apolipoprotein A-I, ubiquitin carboxy terminal hydrolase L1, collapsing response mediator
protein 2 and actin (diluted 1:1,000, Cell Signaling Technology, Beverly, MA, U.S.A.).
Membranes were sequentially reacted with secondary antibody (1:5,000, Pierce). ECL Western
blot analysis system (Amersham Pharmacia Biotech, Piscataway, NJ, U.S.A.) was used for
detection according to the manufacturer’s protocol. The intensity analysis was carried out
using SigmaGel 1.0 (Jandel Scientific, San Rafael, CA, U.S.A.) and SigmaPlot 4.0 (SPSS Inc.,
Point Richmond, CA, U.S.A.).
Reverse transverse-PCR amplification: Total RNA from right cerebral
cortices was extracted using Trizol reagent (Invitrogen, Carlsbad, CA, U.S.A.) following the
manufacturer’s protocol. For reverse transcription, we used Superscript III reverse
transcriptase from Invitrogen following the manufacturer’s manuals. The primer sequences are
represented inTable 1 Sequence of the primers used for PCR amplification
for 5 min, followed by 35 cycles from 94°C for 30 sec, annealing at 54°C for 30 sec and an
extension at 72°C for 1 min and a final extension for 10 min at 72°C. RT-PCR products were
separated on a 1% agarose gel and visualized under UV light. The intensity analysis of
RT-PCR products was carried out using SigmaGel 1.0 (Jandel Scientific) and SigmaPlot 4.0
(SPSS Inc.).
Data analysis: All data are expressed as means ± SEM. The results for each
group were compared by one-way analysis of variance (ANOVA) followed by Student’s
t-test. The difference for comparison was considered significant at
P<0.05.
n=36) were purchased from Samtako Animal Breeding Center (Osan, Korea)
and were randomly divided into a sham-operated group, vehicle-treated group and
resveratrol-treated group (n=12 per group). All procedures for animal use
were approved by the Institutional Animal Care and Use Committee of Gyeongsang National
University (GNU-130723-R0050). Experimental animals were housed at 18–22°C under a 12 hr
light/12 hr dark cycle and had free access to a pellet diet and tap water. Resveratrol (30
mg/kg, Sigma, St. Louis, MO, U.S.A.) was dissolved in 2% dimethyl sulfoxide (DMSO) as
vehicle and was injected intraperitoneally as described previously [19 (link)]. Resveratrol or vehicle was
injected immediately after middle cerebral artery occlusion (MCAO).
Middle cerebral artery occlusion: Rats were anesthetized with sodium
pentobarbital (100 mg/kg), and MCAO was carried out as described previously [21 (link)]. Briefly, the right common
carotid artery, external carotid and internal carotid were exposed through a midline cut. A
4/0 nylon filament with a heated rounded tip was inserted from the external carotid artery
into the internal carotid artery and advanced until the rounded tip occluded the origin of
the middle cerebral artery. Sham-operated animals were subjected to the same procedure,
except for insertion of the filament. At 24 hr after the onset of permanent occlusion,
animals were decapitated, and the right cerebral cortex was isolated.
2-Dimensional gel electrophoresis: Proteomic analysis was carried out as
our previously described method [32 (link)].
Proteins were extracted from the right cerebral cortex by homogenization in buffer solution
(8 M urea, 4% CHAPS, ampholytes and 40 mM Tris–HCl) followed by centrifugation at 16,000 g.
Protein concentration was determined by the Bradford method (Bio-Rad, Hercules, CA, U.S.A.)
according to the manufacturer’s protocol. Immobilized pH gradients (IPG, pH 4–7 and pH 6–9,
17 cm, Bio-Rad) were incubated in rehydration buffer (8 M urea, 2% CHAPS, 20 mM DTT, 0.5%
IPG buffer and bromophenol blue) for 13 hr at room temperature. Assayed protein samples were
loaded on IPG strips (pH 4–7 and 6–9), and isoelectric focusing (IEF) was performed as
follows: 200 V (1 hr), 500 V (1 hr), 1,000 V to 8,000 V (30 min) and 8,000 V (5 hr) using an
IPG phore unit (GE Healthcare, Uppsala, Sweden). Strips were incubated with equilibration
buffer (6 M urea, 30% glycerol, 2% sodium dodecyl sulfate, 50 mM Tris-HCl and bromophenol
blue) and loaded on gradient gels (7.5–17.5%), followed by second-dimension electrophoresis
using Protein-II XI electrophoresis equipment (Bio-Rad). Settings were 5 mA per gel for 2 hr
followed by 10 mA per gel at 10°C.
Silver staining, image analysis and protein identification: Silver
staining was performed as follows: fixation (12% acetic acid and 50% methanol) for 2 hr,
washing with 50% ethanol and then treatment with 0.2% sodium thiosulfate. Gels were washed
with deionized water and stained in silver solution (0.2% silver nitrate). Gels were
developed in 0.2% sodium carbonate solution, and gel images were collected using an Agfar
ARCUS 1200™ scanner (Agfar-Gevaert, Mortsel, Belgium). PDQuest 2-D analysis software
(Bio-Rad) was used to analyze differences in protein spots among the different groups.
Differentially expressed protein spots were excised and destained. Gel particles were
digested in trypsin-containing buffer, and the extracted peptides were analyzed using a
Voyager-DETM STR biospectrometry workstation (Applied Biosystem, Forster City, CA, U.S.A.)
for peptide mass fingerprinting. Database searches were carried out using MS-Fit and
ProFound software. SWISS-PROT and NCBI were used as protein sequence databases.
Western blot analysis: Western blot analysis was carried out as our
previously described method [13 (link),
32 (link)]. Right cerebral cortex was dissolved in lysis
buffer (1 M Tris–HCl, 5 M sodium chloride, 0.5% sodium deoxycholate, 10% sodium dodecyl
sulfate, 1% sodium azide and 10% NP-40). Protein concentration was determined using a
bicinchoninic acid (BCA) kit (Pierce, Rockford, IL, U.S.A.) according to the manufacturer’s
protocol. Equal volumes of protein (30 µg per sample) were electrophoresed
on 10% SDS-PAGE gels, and the proteins were transferred to poly-vinylidene fluoride (PVDF)
membranes (Millipore, Billerica, MA, U.S.A.). To minimize nonspecific binding, membranes
were blocked with skim milk for 1 hr at room temperature. PVDF membranes were washed in
Tris-buffered saline containing 0.1% Tween-20 (TBST) and then incubated with antibodies
against the following proteins: peroxiredoxin-5, isocitrate dehydrogenase [NAD+],
apolipoprotein A-I, ubiquitin carboxy terminal hydrolase L1, collapsing response mediator
protein 2 and actin (diluted 1:1,000, Cell Signaling Technology, Beverly, MA, U.S.A.).
Membranes were sequentially reacted with secondary antibody (1:5,000, Pierce). ECL Western
blot analysis system (Amersham Pharmacia Biotech, Piscataway, NJ, U.S.A.) was used for
detection according to the manufacturer’s protocol. The intensity analysis was carried out
using SigmaGel 1.0 (Jandel Scientific, San Rafael, CA, U.S.A.) and SigmaPlot 4.0 (SPSS Inc.,
Point Richmond, CA, U.S.A.).
Reverse transverse-PCR amplification: Total RNA from right cerebral
cortices was extracted using Trizol reagent (Invitrogen, Carlsbad, CA, U.S.A.) following the
manufacturer’s protocol. For reverse transcription, we used Superscript III reverse
transcriptase from Invitrogen following the manufacturer’s manuals. The primer sequences are
represented in
| Gene | Primer sequences (F, Forward; R, Reverse) | Product size (bp) | |
|---|---|---|---|
| Peroxiredoxin-5 | F: | 5′-GGAGTCCCTGGGGCATTTAC-3′ | 392 |
| R: | 5′-GACATTCTGGTCAGGGCCTC-3′ | ||
| NAD (+)-dependent isocitrate dehydrogenase | F: | 5′-AAAAATCCATGGCGGTTCTGTG-3′ | 404 |
| R: | 5′-GGTCCCCATAGGCGTGTCG-3′ | ||
| Apolipoprotein A-I | F: | 5′-TGTTGGTCGCCTACAGGAAC-3′ | 223 |
| R: | 5′- TCGCGTTTTTGTGAAGCTCG-3′ | ||
| Ubiquitin carboxyl terminal hydrolase isozyme L1 (UCH-L1) | F: | 5′-CTAGGGCTGGAGGAGGAGAC-3′ | 296 |
| R: | 5′-TTGTCCCCTGAAGAGAGAGC-3′ | ||
| Collapsing response mediator protein 2 (CRMP-2) | F: | 5′-TGGTTTCAGCTTGTCTGGTG-3′ | 454 |
| R: | 5′ -TGACAGGAAGGTGCTGACTG-3′ | ||
| β-actin | F: | 5′-GGGTCAGAAGGACTCCTACG-3′ | 238 |
| R: | 5′- TTTCACTGCGGCTGATGTAG-3′ | ||
for 5 min, followed by 35 cycles from 94°C for 30 sec, annealing at 54°C for 30 sec and an
extension at 72°C for 1 min and a final extension for 10 min at 72°C. RT-PCR products were
separated on a 1% agarose gel and visualized under UV light. The intensity analysis of
RT-PCR products was carried out using SigmaGel 1.0 (Jandel Scientific) and SigmaPlot 4.0
(SPSS Inc.).
Data analysis: All data are expressed as means ± SEM. The results for each
group were compared by one-way analysis of variance (ANOVA) followed by Student’s
t-test. The difference for comparison was considered significant at
P<0.05.
The cytoarchitecture of the PFC was studied in ten adult, male mice (strain C57BL/6) of similar weight (approximately 20 g). These control mouse brains were kindly donated and immersion fixed by Dr. H. Manji, NIMH, USA. All animal procedures were in strict accordance with the NIH animal care guidelines. The histological processing of these brains was performed at the laboratory of Dr. Rajkowska. The brains were embedded in 12% celloidin, cut into 40-μm serial sections using a sliding microtome and Nissl (1% cresyl violet) stained. Celloidin was chosen as an embedding medium to allow for the preparation of ‘thick’ sections with clear morphology and high contrast of Nissl-stained neurons and glial cells. In these immersion-fixed brains, any spots showing pycnotic reaction were not incorporated in this study.
In addition to these ten mice, four adult male mice (C57BL/6 strain) were stained for dopamine and four adult male mice for AChE, myelin, and immunohistochemically for SMI, PV and CB. For each staining, a different set of sections with several consecutive sections stained with Nissl at HBMU’s laboratory was used. The antibodies applied were the dopamine (DA) antibody (Geffard et al. 1984 (link)), SMI-32 antibody (Sternberger Monoclonals Inc., Baltimore, MD, USA: monoclonal antibody to one epitope of non-phosphorylated tau neurofilaments, lot number 11), SMI-311antibody (pan-neuronal neurofilament marker cocktail of several monoclonal antibodies for several epitopes of non-phosphorylated tau protein, Sternberger Monoclonals Inc., Baltimore, MD, USA: lot number 9) (SMI antibodies are presently distributed through Covance Research Products, USA), monoclonal anti-CB D-28K antibody (Sigma, St. Louis, MO, USA: product number C-9848, clone number CB-955, lot number 015K4826), and monoclonal anti-PV antibody (Sigma, St. Louis, MO, USA: product number P-3171, clone number PA-235, lot number 026H4824). Mice to be stained for DA were intracardially perfused under deep pentobarbital anesthesia (1 ml/kg body weight, i.p.), with saline followed by fixative. For DA staining, the fixative was 5% glutaraldehyde in 0.05 M acetate buffer at pH 4.0. After perfusion, the brains were immersed in 0.05 Tris containing 1% sodium disulfite (Na2S2O5) at pH 7.2 (De Brabander et al. 1992 (link)). Mouse PFC was sectioned at 40 μm by a vibratome. These sections were stained overnight in a cold room at 4°C using the polyclonal primary antibody sensitive to DA that was raised in the Netherlands Institute for Brain Research (NIBR) (Geffard et al. 1984 (link)), the specificity of which had been demonstrated previously (Kalsbeek et al. 1990 (link)). DA antiserum was diluted 1:2,000 in 0.05 M Tris containing 1% Na2S2O5 and 0.5% Triton X-100, pH 7.2. After overnight incubation, the sections were washed three times with Tris-buffered saline (TBS) and subsequently incubated in the secondary antibody goat–antirabbit, also raised in NIBR at 1:100 for 1 h. After having been rinsed 3× in TBS, it was incubated in the tertiary antibody, peroxidase–antiperoxidase, at 1:1,000 for 60 min. Both the secondary and the tertiary antibodies were diluted in TBS with 0.5% gelatine and 0.5% Triton X-100. For visualization, the sections were transferred into 0.05% diaminobenzidine (DAB; Sigma) with 0.5% nickel ammonium sulfate. The reaction was stopped after a few minutes by transferring the sections to TBS (3 × 10 min), then the sections were mounted on slides, air dried, washed, dehydrated and coverslipped.
Mice to be stained with anti-PV, anti-CB and SMI-32 and SMI-311 were fixed with 4% formaldehyde solution in 0.1 M phosphate buffer at pH 7.6. Mouse PFC was sectioned at 40 μm by a vibratome. To prevent endogenous peroxidase activity, free-floating sections were pretreated for 30 min in a Tris-buffered saline (TBS) solution containing 3% hydrogen peroxide and 0.2% Triton X-100. To prevent non-specific antibody staining, these sections were placed in a milk solution (TBS containing 5% nonfat dry milk and 0.2% Triton X-100) for 1 h. Incubation of the primary antibody, directly after the milk step was carried out overnight in a cold room at 4°C. The primary antibodies were diluted in the above-mentioned milk solution: SMI-32 and SMI-311 at 1:1,000, PV antibody at 1:1,000, and CB antibody at 1:250. For the monoclonal SMI-32, SMI-311, PV and CB antibodies, raised in mice, we used peroxidase-conjugated rabbit–antimouse (1:100 in 5% milk solution with 0.2% Triton X-100) as a secondary antibody. Visualization took place in 0.05% diaminobenzidine enhanced with 0.2% nickel ammonium sulfate. The reaction was stopped after a few minutes by transferring these sections to TBS (3 × 10 min), after which the sections were rinsed in distilled water, mounted on slides, air dried, washed, dehydrated and coverslipped. Control sections that were incubated according to the same procedure as described above, omitting the primary antibody, were all negative. All sections were cut coronally, because the coronal plane offers in general the best view to differentiate between the subareas of the rodent PFC (Uylings et al. 2003 (link); Van de Werd and Uylings 2008 (link)).
Sections were processed for AChE staining according to the protocol described by Cavada et al. (1995 (link)). The sections were incubated overnight in a solution of cupric sulfate and acetate buffer at pH 5 to which acetylthiocholine iodide and ethopropazine were added just before the start of incubation. After rinsing, the sections were developed in a sodium sulfide solution until a light brown color appeared and subsequently intensified to a dark brown color in a silver nitrate solution. Finally, the sections were differentiated after rinsing in a thiosulfate solution, dehydrated and mounted. In all steps, the solutions and sections were shaken constantly. The myelin was stained with silver by physical development according to Gallyas (1979 (link)). The sections were first placed in 100% ethanol and then immersed in a 2:1 solution of pyridine and acetic acid for 30 min. After rinsing, they were placed in an ammonium silver nitrate solution and after rinsing with 0.5% acetic acid, the sections were immersed in the optimal physical developer solution at room temperature (Gallyas 1979 (link)) until they showed good stain intensity under the microscope. Then the development of the staining was stopped in 0.5% acetic acid and the sections were dehydrated and mounted with Histomount. The sections were studied at intervals of 80–160 μm, and examined under a light microscope at a 63× magnification.
In addition to these ten mice, four adult male mice (C57BL/6 strain) were stained for dopamine and four adult male mice for AChE, myelin, and immunohistochemically for SMI, PV and CB. For each staining, a different set of sections with several consecutive sections stained with Nissl at HBMU’s laboratory was used. The antibodies applied were the dopamine (DA) antibody (Geffard et al. 1984 (link)), SMI-32 antibody (Sternberger Monoclonals Inc., Baltimore, MD, USA: monoclonal antibody to one epitope of non-phosphorylated tau neurofilaments, lot number 11), SMI-311antibody (pan-neuronal neurofilament marker cocktail of several monoclonal antibodies for several epitopes of non-phosphorylated tau protein, Sternberger Monoclonals Inc., Baltimore, MD, USA: lot number 9) (SMI antibodies are presently distributed through Covance Research Products, USA), monoclonal anti-CB D-28K antibody (Sigma, St. Louis, MO, USA: product number C-9848, clone number CB-955, lot number 015K4826), and monoclonal anti-PV antibody (Sigma, St. Louis, MO, USA: product number P-3171, clone number PA-235, lot number 026H4824). Mice to be stained for DA were intracardially perfused under deep pentobarbital anesthesia (1 ml/kg body weight, i.p.), with saline followed by fixative. For DA staining, the fixative was 5% glutaraldehyde in 0.05 M acetate buffer at pH 4.0. After perfusion, the brains were immersed in 0.05 Tris containing 1% sodium disulfite (Na2S2O5) at pH 7.2 (De Brabander et al. 1992 (link)). Mouse PFC was sectioned at 40 μm by a vibratome. These sections were stained overnight in a cold room at 4°C using the polyclonal primary antibody sensitive to DA that was raised in the Netherlands Institute for Brain Research (NIBR) (Geffard et al. 1984 (link)), the specificity of which had been demonstrated previously (Kalsbeek et al. 1990 (link)). DA antiserum was diluted 1:2,000 in 0.05 M Tris containing 1% Na2S2O5 and 0.5% Triton X-100, pH 7.2. After overnight incubation, the sections were washed three times with Tris-buffered saline (TBS) and subsequently incubated in the secondary antibody goat–antirabbit, also raised in NIBR at 1:100 for 1 h. After having been rinsed 3× in TBS, it was incubated in the tertiary antibody, peroxidase–antiperoxidase, at 1:1,000 for 60 min. Both the secondary and the tertiary antibodies were diluted in TBS with 0.5% gelatine and 0.5% Triton X-100. For visualization, the sections were transferred into 0.05% diaminobenzidine (DAB; Sigma) with 0.5% nickel ammonium sulfate. The reaction was stopped after a few minutes by transferring the sections to TBS (3 × 10 min), then the sections were mounted on slides, air dried, washed, dehydrated and coverslipped.
Mice to be stained with anti-PV, anti-CB and SMI-32 and SMI-311 were fixed with 4% formaldehyde solution in 0.1 M phosphate buffer at pH 7.6. Mouse PFC was sectioned at 40 μm by a vibratome. To prevent endogenous peroxidase activity, free-floating sections were pretreated for 30 min in a Tris-buffered saline (TBS) solution containing 3% hydrogen peroxide and 0.2% Triton X-100. To prevent non-specific antibody staining, these sections were placed in a milk solution (TBS containing 5% nonfat dry milk and 0.2% Triton X-100) for 1 h. Incubation of the primary antibody, directly after the milk step was carried out overnight in a cold room at 4°C. The primary antibodies were diluted in the above-mentioned milk solution: SMI-32 and SMI-311 at 1:1,000, PV antibody at 1:1,000, and CB antibody at 1:250. For the monoclonal SMI-32, SMI-311, PV and CB antibodies, raised in mice, we used peroxidase-conjugated rabbit–antimouse (1:100 in 5% milk solution with 0.2% Triton X-100) as a secondary antibody. Visualization took place in 0.05% diaminobenzidine enhanced with 0.2% nickel ammonium sulfate. The reaction was stopped after a few minutes by transferring these sections to TBS (3 × 10 min), after which the sections were rinsed in distilled water, mounted on slides, air dried, washed, dehydrated and coverslipped. Control sections that were incubated according to the same procedure as described above, omitting the primary antibody, were all negative. All sections were cut coronally, because the coronal plane offers in general the best view to differentiate between the subareas of the rodent PFC (Uylings et al. 2003 (link); Van de Werd and Uylings 2008 (link)).
Sections were processed for AChE staining according to the protocol described by Cavada et al. (1995 (link)). The sections were incubated overnight in a solution of cupric sulfate and acetate buffer at pH 5 to which acetylthiocholine iodide and ethopropazine were added just before the start of incubation. After rinsing, the sections were developed in a sodium sulfide solution until a light brown color appeared and subsequently intensified to a dark brown color in a silver nitrate solution. Finally, the sections were differentiated after rinsing in a thiosulfate solution, dehydrated and mounted. In all steps, the solutions and sections were shaken constantly. The myelin was stained with silver by physical development according to Gallyas (1979 (link)). The sections were first placed in 100% ethanol and then immersed in a 2:1 solution of pyridine and acetic acid for 30 min. After rinsing, they were placed in an ammonium silver nitrate solution and after rinsing with 0.5% acetic acid, the sections were immersed in the optimal physical developer solution at room temperature (Gallyas 1979 (link)) until they showed good stain intensity under the microscope. Then the development of the staining was stopped in 0.5% acetic acid and the sections were dehydrated and mounted with Histomount. The sections were studied at intervals of 80–160 μm, and examined under a light microscope at a 63× magnification.
Amines
Biotin
Cysteine
Dyes
ferrocyn
maleimide
Microscopy, Fluorescence
neutravidin
Peptides
Proteins
sodium thiosulfate pentahydrate
All mice received two injections of calcein 9 and 2 d before sacrifice. Dissected skeletons were fixed in 3.7% PBS-buffered formaldehyde for 18 h before they were stored in 80% ethanol. To perform non-decalcified histology, we dehydrated a part of the spine (vertebral bodies L1 to L4) in ascending alcohol concentrations, before they were embedded into methylmetacrylate. Using a Microtec rotation microtome (Techno-Med GmbH) we cut 4-µm-thick sections in the sagittal plane. The sections were subsequently stained by von Kossa/van Gieson (for static hisotmorphometry) and toluidine blue (for cellular histomorphometry) staining procedures (Albers et al., 2011 (link)). Whereas the latter staining is achieved by incubation of the sections with 1% toluidine blue solution (pH 4.5) for 30 min, the von Kossa/van Gieson is a multistep procedure staining mineralized bone matrix in black and non-mineralized osteoid in red. More specifically, after staining with 3% silver nitrate for 5 min and incubation in 5% sodium thiosulfate for 5 min, counterstaining with van Gieson solution (0.25% acid fuchsin, 0.5% nitric acid [conc], 10% glycerine, and picric acid to saturation) was performed for a further 20 min. Static and cellular histomorphometry was performed on toluidine blue–stained sections, whereas dynamic histomorphometry for determination of the bone formation rate was performed on nonstained sections. All histomorphometric measurements were performed using the OsteoMeasure histomorphometry system (Osteometrics Inc., USA) according to American Society for Bone and Mineral Research standards (Parfitt et al., 1987 (link)). Here we followed the manufacturer’s instructions by labeling the mineralized and nonmineralized bone surfaces, marking osteoblasts and osteoclasts, or labeling the calcein bands on unstained 12-µm sections for dynamic histomorphometry. TRAP activity staining was performed on decalcified sections that were preincubated in 10 mM sodium tartrate dissolved in 40 mM acetate buffer (pH 5) and then stained with 0.1 mg/ml Naphthol AS-MX Phosphate (#N-5000;) in the same buffer, including 0.6 mg/ml Fast Red Violet LB salt (#F-3881; Sigma-Aldrich). Staining of hyaloid vessels was performed as described previously (Albers et al., 2011 (link)). In brief, eyeballs were fixed in 3.7% PBS-buffered formaldehyde for 18 h, then dehydrated in ascending alcohol concentrations and embedded into paraffin. Sections of 5 µm were cut and stained by the hematoxylin/eosin procedure. For quantification we determined the number of stained hyaloid vessels per section. All histological images were captured at room temperature using a microscope (Axioskop; Carl Zeiss) with a 1.25× (no medium, NA 0.035), 20× (no medium, NA 0.045), or 40× (no medium, NA 0.75) objective fitted with a camera (Axiocam; Carl Zeiss). Image acquisition was performed using Axiovision Software (Carl Zeiss).
Most recents protocols related to «Sodium thiosulfate»
Weigh 0.05 grams of dry potassium iodate (KIO3), dissolve it in a 250 ml Erlenmeyer flask with 50 ml of aqua distillate, stir until homogeneous. Then add 10 ml of 20% potassium iodide and 2.5 ml of 4 N HCl, then titrate with 0.1 N sodium thiosulfate solution until the solution is yellow, add 2 ml of 1% starch solution and continue titrating until the blue color disappears.
Two investigators (LH and YZL) identified the studies through a systematic search of PubMed, Web of Science, the Cochrane Register of Controlled Trials databases, Embase and China National Knowledge Infrastructure (CNKI) databases from inception to November 2022, using the following search terms: vascular calcification, sodium thiosulfate, cinacalcet, bisphosphonates, randomized clinical trials (RCTs) and their medical subject heading (MeSH) terms with the Boolean search terms ‘OR’ and ‘AND’. The details of the search strategy were presented in the Supplementary Table 1 .
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By heating the pulp with 12% hydrochloric acid, the polysaccharide in the pulp (α-cellulose) was converted to furfural.
The content of pentose was obtained from the empirical formula by calculating the amount of furfural. The formulae for both are given below:
X1—Content of furfural, %;
X2—Content of pentose, %;
1.375—Conversion of furfural to pentose;
A—The amount of furfural equivalent to 1 mL 1 mol/L sodium thiosulfate standard solution, A (Tetrabromination) = 0.024;
V1—Consumption of standard sodium thiosulfate solution during blank test, mL;
V2—Consumption of standard sodium thiosulfate solution for titrating samples, mL;
c—Concentration of sodium thiosulfate standard solution, mol/L;
m—Quality of dry test sample, g.
The content of pentose was obtained from the empirical formula by calculating the amount of furfural. The formulae for both are given below:
X1—Content of furfural, %;
X2—Content of pentose, %;
1.375—Conversion of furfural to pentose;
A—The amount of furfural equivalent to 1 mL 1 mol/L sodium thiosulfate standard solution, A (Tetrabromination) = 0.024;
V1—Consumption of standard sodium thiosulfate solution during blank test, mL;
V2—Consumption of standard sodium thiosulfate solution for titrating samples, mL;
c—Concentration of sodium thiosulfate standard solution, mol/L;
m—Quality of dry test sample, g.
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Example 1
Poloxamer 407 Gel 1 (0.1 M STS, 20% (w/v) Poloxamer 407)
Sodium thiosulfate pentahydrate (106.07 mg) was dissolved in sterile, distilled water (4.274 mL) in a sterile vial to produce a clear solution. Poloxamer 407 (855 mg; purified, non-ionic, Sigma-Aldrich) was added into the solution, and the resulting mixture was stirred for 15-20 min at 4° C. Evans blue (4.27 mg) was added into the vial and stirred for 10 mins at 4° C. (ice/water bath).
Poloxamer 407 Gel 2 (0.5M STS, 16% (w/v) Poloxamer 407)
Poloxamer 407 gel 2 was prepared according to the procedure described for Poloxamer 407 gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 0.5M concentration of sodium thiosulfate, and the amount of poloxamer 407 was adjusted to provide a 16% (w/v) concentration of poloxamer 407.
Preparation of Poloxamer 407 gels with 0.6M-0.8M STS, 16% (w/v) poloxamer 407 led to the observation of precipitation without gel formation.
Hyaluronan Gel 1 (0.5M STS, 1% (w/v) hyaluronan)
Sodium thiosulfate pentahydrate (619.75 mg) was dissolved in sterile, distilled water (5 mL) in a sterile vial to produce a clear solution. Hyaluronan (50.30 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to the solution, and the resulting mixture was stirred for 8-10 min at 4° C. The resulting solution was filtered through 0.22 μm Millex-GV sterile filter.
Hyaluronan Gel 2 (0.1M STS, 2% (w/v) Hyaluronan)
Sodium thiosulfate pentahydrate (124.87 mg) was dissolved in sterile, distilled water (3.031 mL). Methylcellulose (351.01 mg; Methocel® A15 Premium LV, Dow Chemical Company) was dissolved in sterile, distilled water (2.0 mL), and the resulting solution was mixed with the sodium thiosulfate solution. Hyaluronan (100.10 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to the resulting mixture and mixed at 4° C. for 10-15 min.
Hyaluronan Gel 3 (0.5M STS, 2% (w/v) Hyaluronan)
Sodium thiosulfate pentahydrate (620.35 mg) was dissolved in sterile, distilled water (3 mL). Methylcellulose (350.23 mg; Methocel® A15 Premium LV, Dow Chemical Company) was dissolved in sterile, distilled water (2.0 mL), and the resulting solution was mixed with the sodium thiosulfate solution. Hyaluronan (100.65 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to the resulting mixture and mixed at 4° C. for 10-15 min.
Hyaluronan Gel 4 (0.1M STS, 1% (w/v) Hyaluronan, Manitol)
Hyaluronan (50.09 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to water (5 mL). Sodium thiosulfate pentahydrate (124.9 mgs) was added. The pH of the resulting mixture was adjusted to pH7.12 by addition of sodium hydroxide (1N, ca. 0.5 μL). Add appropriate amount of mannitol into the vial to adjust the osmolarity to 1.046 Osm/kg. The viscous solution was filtered through 0.22 μm Millex-GV filter.
Hyaluronan Gel 5 (0.1M STS, 1% (w/v) Hyaluronan)
Hyaluronan Gel 5 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 0.1 M concentration of sodium thiosulfate.
Hyaluronan Gel 6 (0.2M STS, 1% (w/v) Hyaluronan)
Hyaluronan Gel 6 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 0.2M concentration of sodium thiosulfate.
Hyaluronan Gel 7 (0.3M STS, 1% (w/v) Hyaluronan)
Hyaluronan Gel 7 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 0.3M concentration of sodium thiosulfate.
Hyaluronan Gel 8 (0.4M STS, 1% (w/v) Hyaluronan)
Hyaluronan Gel 8 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 0.4M concentration of sodium thiosulfate.
Hyaluronan Gel 9 (0.5M STS, 1% (w/v) Hyaluronan, Tris (5×))
Hyaluronan (79.99 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to Tris buffer (8 mL, AMRESCO-0497-500G). The pH of the resulting mixture was adjusted to pH7.13 by addition of HCl (5N). Sodium thiosulfate pentahydrate (992.60 mg) was added to the above solution. The viscous solution was filtered through 0.22 μm Millex-GV filter.
Hyaluronan Gel 10 (0.5M STS, 1% (w/v) Hyaluronan, Phosphate Buffered Saline (5×))
Hyaluronan (70.38 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to PBS buffer (7 mL, 5×). Sodium thiosulfate pentahydrate (868.46 mg) was added. The pH of the resulting mixture was adjusted to pH6.99 by addition of NaOH (1N). The viscous solution was filtered through 0.22 μM Millex-GV filter.
Hyaluronan Gel 11 (0.8M STS, 1% (w/v) Hyaluronan)
Hyaluronan Gel 11 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 0.8M concentration of sodium thiosulfate.
Hyaluronan Gel 12 (1M STS, 0.8% (w/v) Hyaluronan)
Hyaluronan Gel 12 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 1M concentration of sodium thiosulfate, and the amount of hyaluronan was adjusted to provide a 0.8% (w/v) concentration of hyaluronan.
Hyaluronan Gel 13 (0.5M STS, 0.82% (w/v) Hyaluronan (HYALGAN))
Hyaluronan Gel 13 was prepared by mixing of sodium thiosulfate pentahydrate with hyaluronan (HYALGAN, Fidia Pharma USA, Florham Park, NJ) to afford the final preparation with 0.82% (w/v) concentration of hyaluronan.
Hyaluronan Gel 14 (0.5M STS, 1% (w/v) Hyaluronan (SINGCLEAN))
Hyaluronan Gel 14 was prepared according to the procedure described for Hyaluronan Gel 13 with the exception that hyaluronan (SINGCLEAN, Hangzhouh Singclean Medical Products Co., Ltd., Hangzhou, China) was used in the preparation of this gel.
Hyaluronan Gel 15 (0.5M STS, 1% (w/v) Hyaluronan (EUFLEXXA))
Hyaluronan Gel 15 was prepared according to the procedure described for Hyaluronan Gel 13 with the exception that hyaluronan (EUFLEXXA, Ferring Pharmaceuticals Inc., Parsippany, NJ) was used in the preparation of this gel.
Hyaluronan Gel 16 (0.5M STS, 1% (w/v) Hyaluronan (HEALON))
Hyaluronan Gel 16 was prepared according to the procedure described for Hyaluronan Gel 13 with the exception that hyaluronan (HEALON, Johnson & Johnson, New Brunswick, NJ) was used in the preparation of this gel.
Hyaluronan Gel 17 (1M STS, 1% (w/v) Hyaluronan)
Hyaluronan Gel 17 was prepared according to the procedure described for Hyaluronan Gel 1 with the exception that the amount of sodium thiosulfate pentahydrate was adjusted to provide a 1M concentration of sodium thiosulfate.
Hyaluronan Gel 18 (10% (w/v) N-Acetyl-L-Cysteine, 1% (w/v) Hyaluronan)
Hyaluronan (39.38 mg; Pharma Grade 80, Kikkoman Biochemifa company; 0.6-1.2 mDa) was added to water (4 mL). N-Acetyl-L-cysteine (399.14 mg) was added. The pH of the resulting mixture was adjusted to pH 7.21 by addition of NaOH (10N, 240 μL). The viscous solution was filtered through 0.22 μM Millex-GV filter. The osmotic pressure was measured as 1.107 Osm/kg.
Other hyaluronan gels may be prepared using the procedures described herein. For example, 1M and 1.5M hyaluronan gels may be prepared according to the same procedure as described for, e.g., Hyaluronan Gel 1 and Hyaluronan Gel 12. Additionally, pH levels of the gels may be adjusted to pH 6.5 to 8.5 using Brønsted acids (e.g., hydrochloric acid) and bases (e.g., sodium hydroxide).
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Oxygen barrier property was measured by sodium thiosulfate titration [13 (link)]. First, 3 g of soybean oil was placed into 50 mL conical bottles of the same size. These conical bottles were then sealed with different composite membranes. One bottle without a membrane seal was designated as the blank group. All the films were subsequently placed in an incubator at 50 °C for 3 days, after which the peroxide value (PV) was measured. The peroxide value of the oil was determined in accordance with GB 5009.227. The PV was calculated using the following formula:
In the formula, PV is the peroxide value, g/100 g; V is the volume of sodium thiosulfate standard solution consumed by the sample, mL; V0 is the volume of sodium thiosulfate standard solution consumed in the blank sample, mL; c is the concentration of sodium thiosulfate standard solution, mol/L; 0.1269 is the mass of iodine equivalent to 1.00 mL of standard titration solution of sodium thiosulfate, [c(Na2S2O3)] = 1.000 mol/L; m is the sample mass, g; and 100 is the conversion factor.
In the formula, PV is the peroxide value, g/100 g; V is the volume of sodium thiosulfate standard solution consumed by the sample, mL; V0 is the volume of sodium thiosulfate standard solution consumed in the blank sample, mL; c is the concentration of sodium thiosulfate standard solution, mol/L; 0.1269 is the mass of iodine equivalent to 1.00 mL of standard titration solution of sodium thiosulfate, [c(Na2S2O3)] = 1.000 mol/L; m is the sample mass, g; and 100 is the conversion factor.
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Sodium thiosulfate is a chemical compound commonly used in laboratory settings. It has a chemical formula of Na2S2O3 and is a colorless, crystalline solid. The primary function of sodium thiosulfate is as a reducing agent and a fixing agent in various analytical and photographic processes.
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More about "Sodium thiosulfate"
Sodium thiosulfate (Na2S2O3) is a versatile chemical compound with a wide range of applications in research and industry.
It is commonly used as a reducing agent, a fixative in photography, and a treatment for certain medical conditions.
Sodium thiosulfate is known for its ability to react with various substances, including potassium iodide, silver nitrate, and methanol.
It can be used as a reducing agent in chemical reactions, helping to convert substances from one oxidation state to another.
In the field of photography, sodium thiosulfate is a key component of the fixing process, which helps stabilize and preserve photographic images.
In the medical field, sodium thiosulfate has been used to treat conditions such as cyanide poisoning, heavy metal toxicity, and certain skin conditions.
It can also be used as a preservative and stabilizer in various pharmaceutical and personal care products.
Researchers can leverage PubCompare.ai's AI-driven platform to discover the power of sodium thiosulfate by locating the best research protocols from literature, pre-prints, and patents through comprehensive search.
The platform's AI-driven comparisons can help users optimize their workflow and identify the most effective protocols and products, allowing them to experience the future of research today.
In addition to its primary uses, sodium thiosulfate has also been explored for its potential applications in the production of ethanol, as a component in hydrochloric acid solutions, and as a precursor for the synthesis of chloroform and acetic acid.
Its versatility and wide-ranging applications make it an important chemical compound in both research and industry.
It is commonly used as a reducing agent, a fixative in photography, and a treatment for certain medical conditions.
Sodium thiosulfate is known for its ability to react with various substances, including potassium iodide, silver nitrate, and methanol.
It can be used as a reducing agent in chemical reactions, helping to convert substances from one oxidation state to another.
In the field of photography, sodium thiosulfate is a key component of the fixing process, which helps stabilize and preserve photographic images.
In the medical field, sodium thiosulfate has been used to treat conditions such as cyanide poisoning, heavy metal toxicity, and certain skin conditions.
It can also be used as a preservative and stabilizer in various pharmaceutical and personal care products.
Researchers can leverage PubCompare.ai's AI-driven platform to discover the power of sodium thiosulfate by locating the best research protocols from literature, pre-prints, and patents through comprehensive search.
The platform's AI-driven comparisons can help users optimize their workflow and identify the most effective protocols and products, allowing them to experience the future of research today.
In addition to its primary uses, sodium thiosulfate has also been explored for its potential applications in the production of ethanol, as a component in hydrochloric acid solutions, and as a precursor for the synthesis of chloroform and acetic acid.
Its versatility and wide-ranging applications make it an important chemical compound in both research and industry.