Human breast epithelial cells (MCF10A) were transfected with a pQCXIH vector and were cultured in DMEM/F12 (Invitrogen, Carlsbad, CA) supplemented with 5% horse serum (Invitrogen), 20 ng/mL EGF, 0.5 μg/mL hydro-cortisone, 100 ng/mL cholera toxin, 10 μg/mL insulin, and 50 μg/mL penicillin/streptomycin until 70–80% confluence was reached. The cells were then lysed in a buffer containing 8 M urea, 2.5 mM sodium pyrophosphate, 1 mM β-glycerophosphate, 50 mM ammonium bicarbonate, one-third tablet of protease inhibitor, and 2 mM sodium ortho-vanadate. Proteins were denatured, reduced, and alkylated after which tryptic digestions were performed at an enzyme/substrate ratio of 1:50. For method comparison between SCX and RP, digested peptides were cleaned by flowing through a 1 mL solid-phase extraction C18 column (Discovery DSC-18, SUPELCO, Bellefonte, PA). Samples were concentrated using a Speed-Vac SC 250 Express (Thermo Savant, Holbrook, NY) and stored at −80°C until time for analysis. A 300.0 μg desalted peptide sample was used for each SCX, low-pH RPLC, and high-pH RPLC fractionation. A 300.0 μg nondesalted protein digest was used to evaluate the potential of high-pH approach for desalting.
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Sodium glycerophosphate
Sodium glycerophosphate
Sodium glycerophosphate is a water-soluble salt of glycerophosphoric acid and sodium.
It is used in various pharmaceutical and biomedical applications, such as a buffer in cell culture media and a source of organic phosphate for bone and tissue regeneration.
Sodium glycerophosphate has also been investigated for its potential neuroprotective and anti-inflammatory properties.
Researchers can explore protocols and products related to this compound using the AI-powered search and comparison tools provided by PubCompare.ai to enhance the reproducibility and accuracy of their studies.
It is used in various pharmaceutical and biomedical applications, such as a buffer in cell culture media and a source of organic phosphate for bone and tissue regeneration.
Sodium glycerophosphate has also been investigated for its potential neuroprotective and anti-inflammatory properties.
Researchers can explore protocols and products related to this compound using the AI-powered search and comparison tools provided by PubCompare.ai to enhance the reproducibility and accuracy of their studies.
Most cited protocols related to «Sodium glycerophosphate»
ammonium bicarbonate
beta-glycerol phosphate
Breast
Buffers
Cells
Cholera Toxin
Cloning Vectors
Cortisone
Digestion
Enzymes
Epithelial Cells
Equus caballus
Fractionation, Chemical
Homo sapiens
Insulin
Penicillins
Peptides
Protease Inhibitors
Proteins
Serum
sodium pyrophosphate
Sodium Vanadate
Solid Phase Extraction
Streptomycin
Tablet
Trypsin
Urea
Antibodies
Antibodies, Anti-Idiotypic
beta-glycerol phosphate
Biological Assay
Buffers
Cells
Complex, Immune
Densitometry
Edetic Acid
Gels
Glycerin
HEPES
Homo sapiens
Immunoprecipitation
Jurkat Cells
Magnesium Chloride
manganese chloride
myosin phosphatase-Rho interacting protein, human
NADH Dehydrogenase Complex 1
Nonidet P-40
Orthovanadate
Phosphotransferases
Rabbits
SDHD protein, human
Sepharose
Sodium
Sodium Chloride
Tromethamine
Wild type yeast (Saccharomyces cerevisiae) strain SUB62 (MATa his3-Δ200 lys2–801 leu2–3, 112 trp1–1 ura3–52) was cultured in synthetic complete medium. At OD600 1, cells were harvested by addition of sodium azide to a final concentration of 10 mM, followed by centrifugation at 1,700 × g (Eppendorf), washed once with cold deionized water, pelleted and snap frozen at −80 °C. Pellets were thawed and resuspended in modified RIPA buffer containing 150 mM NaCl, 1% Nonidet P-40, 0.5% sodium deoxycholate, 0.1% SDS, 50 mM Tris-HCl pH 8.0, 5 mM DTT, and yeast specific protease inhibitor (Sigma-Aldrich). Cells were mechanically lysed using a minibead beater (BioSpec Products) as previously described,10 (link) where cells were beaten with 1 mL of chilled zirconia beads (Biospec Products) in four 30 s cycles, with 30 s rest on ice between cycles.
HeLa cells were maintained in Dulbecco’s modified Eagle’s medium (Invitrogen) supplemented with 10% dialyzed fetal bovine serum (HyClone, Thermo Scientific). For cell lysis, the media was removed, the cells harvested by scraping, the cell pellet was washed with ice-cold PBS and then lysed with ice-cold lysis buffer composed of 10 mM K2HPO4 pH 7.5, 1 mM EDTA, 10 mM MgCl2, 50 mM β-glycerophosphate, 5 mM EGTA, 0.5% Nonidet P-40, 0.1% Brij 35, 0.1% sodium deoxycholate, 1 mM sodium orthovanadate, 1 mM PMSF, 5 μg/ml leupeptin and 5 μg/ml pepstatin A. The lysate was centrifuged at 20,000 × g for 10 min to remove cell debris.
HeLa cells were maintained in Dulbecco’s modified Eagle’s medium (Invitrogen) supplemented with 10% dialyzed fetal bovine serum (HyClone, Thermo Scientific). For cell lysis, the media was removed, the cells harvested by scraping, the cell pellet was washed with ice-cold PBS and then lysed with ice-cold lysis buffer composed of 10 mM K2HPO4 pH 7.5, 1 mM EDTA, 10 mM MgCl2, 50 mM β-glycerophosphate, 5 mM EGTA, 0.5% Nonidet P-40, 0.1% Brij 35, 0.1% sodium deoxycholate, 1 mM sodium orthovanadate, 1 mM PMSF, 5 μg/ml leupeptin and 5 μg/ml pepstatin A. The lysate was centrifuged at 20,000 × g for 10 min to remove cell debris.
beta-glycerol phosphate
Brij 35
Buffers
Cell Cycle
Cells
Centrifugation
Cold Temperature
Deoxycholic Acid, Monosodium Salt
Eagle
Edetic Acid
Egtazic Acid
Fetal Bovine Serum
Freezing
HeLa Cells
leupeptin
Magnesium Chloride
Nonidet P-40
Orthovanadate
Pellets, Drug
pepstatin
potassium phosphate, dibasic
Protease Inhibitors
Radioimmunoprecipitation Assay
Saccharomyces cerevisiae
Sodium
Sodium Azide
Sodium Chloride
Strains
Tromethamine
tyrosinase-related protein-1
Yeast, Dried
zirconium oxide
RNAse III-deficient HT115 bacteria were transformed with an L4440-derived plasmid, corresponding to the required RNAi treatment. A 0.5ml pre-culture was then grown overnight, and used to inoculate a 400 ml culture in ‘Terrific Broth’ (12 g/l Tryptone, 24 g/l yeast extract, 9.4 g/l K2HPO4, 2.2 g/l KH2PO4, adjusted to pH 7). After 7 hours of growth in a baffled flask at 37°C with agitation, expression of dsRNA was induced overnight at 20°C by addition of 3mM IPTG. The bacteria were then pelleted and resuspended with one-fifth volume of buffer (M9 medium supplemented with 75 mg/l cholesterol; 100 mg/l ampicillin; 50 mg/l tetracycline; 12.5 mg/l amphotericin B; 3 mM IPTG).
For each experiment, 1ml of a synchronized population of L4 worms expressing GFP-PSF-1 were fed for 50 hours at 20°C on a 15 cm RNAi plate (see above), supplemented with 8 g of bacterial pellet for the required RNAi treatment, prepared as described above. After feeding, the adults worms were washed in M9 medium and resuspended for 2 minutes at room temperature in 14 ml of ‘bleaching solution’ (for 100 ml: 36.5 ml H2O, 45.5 ml 2N NaOH and 18 ml ClNaO 4%), then pelleted for 1 minute at 300 g. This bleaching procedure was repeated two more times, corresponding to a total of 8-12 minutes in bleaching solution, in order to lyse the adult worms and release embryos (about 0.6-0.8 g). After bleaching, the embryos were washed twice with M9 medium.
The remaining steps were performed at 4°C and are based on our previously described methods for isolating protein complexes from yeast cells 1 (link), 10 (link). Embryos were washed twice with lysis buffer (100 mM HEPES-KOH pH 7.9, 50 mM potassium acetate, 10 mM magnesium acetate, 2 mM EDTA), and then resuspended with three volumes of lysis buffer that was supplemented with 2 mM sodium fluoride, 2 mM sodium β-glycerophosphate pentahydrate, 1 mM dithiothreitol (DTT), 1% Protease Inhibitor Cocktail (P8215, Sigma-Aldrich), and 1X ‘Complete Protease Inhibitor Cocktail’ (05056489001, Roche; one tablet dissolved in 1 ml water makes a 25× stock solution). The mixture was transferred drop-wise into liquid nitrogen to prepare ‘popcorn’, which was stored at -80°C. We then ground ~2.5 g of the frozen popcorn in a SPEX SamplePrep 6780 Freezer/Mill. After thawing, we added one-quarter volume of ‘glycerol mix’ buffer (lysis buffer supplemented with 50% glycerol, 300 mM potassium acetate, 0.5% detergent IGEPAL CA-630, protease inhibitors, and DTT at the concentrations mentioned above). De-ubiquitylase enzymes were inhibited by addition of 5µM Ubiquitin PrG (prepared by Axel Knebel and Clare Johnson, MRC PPU, Dundee), and chromosomal DNA was digested with 1600 U of Pierce Universal Nuclease (123991963, Fisher) for 30 minutes at 4°C. Extracts were centrifuged at 25000 g for 30 minutes and then for 100000 g for 1 hour, before pre-incubation with agarose beads (0.4 ml slurry) for 45 minutes. At this point, 50 µl of extract was added to 100 µl of 1.5X Laemmli buffer and stored at -80°C. The remainder of the extracts were then incubated for 90 minutes with 40 µl of GFP-Trap_A beads (Chromotek). The beads were washed four times with 1 ml of wash buffer (100 mM HEPES-KOH pH 7.9, 100 mM potassium acetate, 10 mM magnesium acetate, 2 mM EDTA, 0.1% IGEPAL CA-630, 2 mM sodium fluoride, 2 mM sodium β-glycerophosphate pentahydrate, plus protease inhibitors as above) and bound proteins were eluted at 95°C for 5 min in 100 µl of 1x Laemmli buffer (or 50 µl when used for mass spectrometry analysis) and stored at -80°C.
For each experiment, 1ml of a synchronized population of L4 worms expressing GFP-PSF-1 were fed for 50 hours at 20°C on a 15 cm RNAi plate (see above), supplemented with 8 g of bacterial pellet for the required RNAi treatment, prepared as described above. After feeding, the adults worms were washed in M9 medium and resuspended for 2 minutes at room temperature in 14 ml of ‘bleaching solution’ (for 100 ml: 36.5 ml H2O, 45.5 ml 2N NaOH and 18 ml ClNaO 4%), then pelleted for 1 minute at 300 g. This bleaching procedure was repeated two more times, corresponding to a total of 8-12 minutes in bleaching solution, in order to lyse the adult worms and release embryos (about 0.6-0.8 g). After bleaching, the embryos were washed twice with M9 medium.
The remaining steps were performed at 4°C and are based on our previously described methods for isolating protein complexes from yeast cells 1 (link), 10 (link). Embryos were washed twice with lysis buffer (100 mM HEPES-KOH pH 7.9, 50 mM potassium acetate, 10 mM magnesium acetate, 2 mM EDTA), and then resuspended with three volumes of lysis buffer that was supplemented with 2 mM sodium fluoride, 2 mM sodium β-glycerophosphate pentahydrate, 1 mM dithiothreitol (DTT), 1% Protease Inhibitor Cocktail (P8215, Sigma-Aldrich), and 1X ‘Complete Protease Inhibitor Cocktail’ (05056489001, Roche; one tablet dissolved in 1 ml water makes a 25× stock solution). The mixture was transferred drop-wise into liquid nitrogen to prepare ‘popcorn’, which was stored at -80°C. We then ground ~2.5 g of the frozen popcorn in a SPEX SamplePrep 6780 Freezer/Mill. After thawing, we added one-quarter volume of ‘glycerol mix’ buffer (lysis buffer supplemented with 50% glycerol, 300 mM potassium acetate, 0.5% detergent IGEPAL CA-630, protease inhibitors, and DTT at the concentrations mentioned above). De-ubiquitylase enzymes were inhibited by addition of 5µM Ubiquitin PrG (prepared by Axel Knebel and Clare Johnson, MRC PPU, Dundee), and chromosomal DNA was digested with 1600 U of Pierce Universal Nuclease (123991963, Fisher) for 30 minutes at 4°C. Extracts were centrifuged at 25000 g for 30 minutes and then for 100000 g for 1 hour, before pre-incubation with agarose beads (0.4 ml slurry) for 45 minutes. At this point, 50 µl of extract was added to 100 µl of 1.5X Laemmli buffer and stored at -80°C. The remainder of the extracts were then incubated for 90 minutes with 40 µl of GFP-Trap_A beads (Chromotek). The beads were washed four times with 1 ml of wash buffer (100 mM HEPES-KOH pH 7.9, 100 mM potassium acetate, 10 mM magnesium acetate, 2 mM EDTA, 0.1% IGEPAL CA-630, 2 mM sodium fluoride, 2 mM sodium β-glycerophosphate pentahydrate, plus protease inhibitors as above) and bound proteins were eluted at 95°C for 5 min in 100 µl of 1x Laemmli buffer (or 50 µl when used for mass spectrometry analysis) and stored at -80°C.
RPMI 1640 supplemented with 10% fetal bovine serum (FBS) (Gemini Bio-Products, CA, USA) was used for the cultures of human NK cells and monocytes. OSCCs and stem-like OSCSCs were isolated from oral cancer patient tongue tumors at UCLA, and cultured in RPMI 1640 supplemented with 10% FBS (Gemini Bio-Products, CA, USA), 1.4% antibiotic antimycotic, 1% sodium pyruvate, 1.4% non-essential amino acids, 1% l -glutamine, 0.2% gentamicin (Gemini Bio-Products, CA, USA), and 0.15% sodium bicarbonate (Fisher Scientific, PA, USA). Mia-Paca-2 (MP2) were cultured in DMEM with 10% FBS and 1% penicillin and streptomycin (Gemini Bio-Products, CA, USA). Dental pulp stem cells (DPSCs) and stem cell of apical papillae (SCAP) were cultured in DMEM complete medium supplemented with 2% FBS and 1% penicillin and streptomycin (Gemini Bio-Products, CA, USA). To induce differentiation of DPSCs, they were cultured with DMEM in the presence of ascorbic acid (50 μg/ml), Na-β-glycerophosphate (10 mM) (Sigma Aldrich, MO, USA), and dexamethasone (10−8 M).
Recombinant IL-2 was obtained from NIH-BRB. Recombinant TNF-α and IFN-γ were obtained from BioLegend (San Diego, CA, USA). The anti-B7H1 was a generous gift from Dr. Liping Chen. Antibodies to CD16, CD54, and LFA-1 were purchased from BioLegend (San Diego, CA, USA). Anti-MHC class I were prepared in our laboratory and 1:100 dilution was found to be the optimal concentration to use. PE – anti-CD26, anti-CD54, anti-CD44, anti-B7H1, anti-CD166, anti-CD326, and anti-CD338 were obtained from BioLegend (San Diego, CA, USA). Antibodies to TNF-α and IFN-γ were prepared in our laboratory and 1:100 dilution was found to be the optimal concentration to use. The human NK and monocyte purification kits were obtained from Stem Cell Technologies (Vancouver, BC, Canada). Cisplatin was obtained through Ronald Reagan Pharmacy at UCLA. Monensin was purchased through BioLegend (San Diego, CA, USA). Propidium iodide (PI) is purchased from Sigma Aldrich (Buffalo, NY, USA).
Recombinant IL-2 was obtained from NIH-BRB. Recombinant TNF-α and IFN-γ were obtained from BioLegend (San Diego, CA, USA). The anti-B7H1 was a generous gift from Dr. Liping Chen. Antibodies to CD16, CD54, and LFA-1 were purchased from BioLegend (San Diego, CA, USA). Anti-MHC class I were prepared in our laboratory and 1:100 dilution was found to be the optimal concentration to use. PE – anti-CD26, anti-CD54, anti-CD44, anti-B7H1, anti-CD166, anti-CD326, and anti-CD338 were obtained from BioLegend (San Diego, CA, USA). Antibodies to TNF-α and IFN-γ were prepared in our laboratory and 1:100 dilution was found to be the optimal concentration to use. The human NK and monocyte purification kits were obtained from Stem Cell Technologies (Vancouver, BC, Canada). Cisplatin was obtained through Ronald Reagan Pharmacy at UCLA. Monensin was purchased through BioLegend (San Diego, CA, USA). Propidium iodide (PI) is purchased from Sigma Aldrich (Buffalo, NY, USA).
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Most recents protocols related to «Sodium glycerophosphate»
Buffer A: 50 mM β-glycerophosphate (pH 7.3), 1.5 mM EGTA, 1 mM EDTA, 1 mM dithiothreitol, and 0.1 mM sodium vanadate. Buffer H: 50 mM β-glycerophosphate, pH 7.3, 1.5 mM EGTA, 1 mM EDTA, 1 mM DTT, 0.1 mM sodium vanadate, 1 mM benzamidine, 10 µg/ml aprotinin, 10 µg/ml leupeptin, and 2 µg/ml pepstatin A. Coimmunoprecipitation (CoIP) buffer: 20 mM HEPES pH 7.4, 2 mM MgCl2, 2 mM EGTA, 150 mM NaCl and 0.1% Triton.
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Sodium salts of butyrate, propionate, acetate, formate, and disodium succinate, disodium β-glycerophosphate pentahydrate, and L-ascorbic acid phosphate magnesium salt n-hydrate were purchased from Fujifilm Wako (Osaka, Japan). Sodium isobutyrate and sodium isovalerate were purchased from Kanto Chemical (Tokyo, Japan) and sodium lactate from Sigma Aldrich (St. Louis, MO, USA).
DMEM osteogenic induction medium is composed of the following: dexamethasone 10 µg, vitamin C 25 mg, β-sodium glycerophosphate 1.08 g, and DMEM 500 mL.
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Transfected cells were lysed in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris, pH 7.3, 0.25 mM EDTA, 1% sodium deoxycholate, 1% Trition-X 100, 0.2% sodium fluoride, 5 mM sodium orthovanadate, 25 mM sodium glycerophosphate and cocktail protease inhibitors (Roche Applied Science, Germany). anti-FLAG M2 beads (Sigma-Aldrich, St Louis, USA) or Magnetic anti-HA beads (Pierce, Thermo Fisher Sci, USA) were used to immunoprecipitate FLAG-tagged or HA-tagged protein, respectively. Bound protein partners of the precipitated proteins were analyzed by western blotting. Blots were probed with anti-FLAG (Sigma-Aldrich, St Louis, USA), anti-HA (Invitrogen, USA), anti-pY antibodies 4G10-platinum (Merck Millipore, USA).
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The 193 bp 601 DNA fragment was amplified by a PCR reaction (62 (link), 63 (link)). The nucleosomes were assembled with the salt dialysis method described above. The reconstituted nucleosome was dialyzed into buffer XL (80 mM PIPES-KOH [pH 6.8], 15 mM NaCl, 60 mM KCl, 30 % glycerol, 1 mM EGTA, 1 mM MgCl2, 10 mM β-glycerophosphate, 10 mM sodium butyrate). H1.8-GFP was mixed with nucleosome with a 1.25 molar ratio in the presence of 0.001 % poly L-glutamic acid (wt 3,000–15,000) (Sigma-Aldrich) and incubated at 37 °C for 30 min. As a control nucleosome sample without H1.8-GFP, the sample without H1.8-GFP was also prepared. The samples were then crosslinked adding a 0.5-time volume of buffer XL containing 3 % formaldehyde and incubating for 90 min on ice. The crosslink reaction was quenched by adding 1.7 volume of quench buffer (30 mM HEPES-KOH (pH 7.4), 150 mM KCl, 1 mM EGTA, 10 ng/μL leupeptin, 10 ng/μL pepstatin, 10 ng/μL chymostatin, 10 mM sodium butyrate, 10 mM β-glycerophosphate, 400 mM glycine, 1 mM MgCl2, 5 mM DTT). The quenched sample was layered onto the 10–25 % linear sucrose gradient solution with buffer SG (15 mM HEPES-KOH [pH 7.4], 50 mM KCl, 10–22 % sucrose, 10 μg/ml leupeptin, 10 μg/ml pepstatin, 10 μg/ml chymostatin, 10 mM sodium butyrate, 10 mM β-glycerophosphate, 1 mM EGTA, 20 mM glycine) and spun at 32,000 rpm (max 124,436 rcf) and 4 °C for 13 h using SW55Ti rotor in Optima L80 (Beckman Coulter). The centrifuged samples were fractionated from the top of the sucrose gradient. The concertation of H1.8-GFP bound nucleosome in each fraction is calculated based on the 260 nm light absorbance detected by Nanodrop 2000 (Thermo Scientific).
Top products related to «Sodium glycerophosphate»
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Dexamethasone is a synthetic glucocorticoid medication used in a variety of medical applications. It is primarily used as an anti-inflammatory and immunosuppressant agent.
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β-glycerophosphate is a chemical compound that serves as a buffering agent and source of phosphate for cell culture media. It helps maintain a stable pH environment for cell growth and proliferation.
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The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.
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Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.
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Ascorbic acid is a chemical compound commonly known as Vitamin C. It is a water-soluble vitamin that plays a role in various physiological processes. As a laboratory product, ascorbic acid is used as a reducing agent, antioxidant, and pH regulator in various applications.
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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
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Sodium β-glycerophosphate is a laboratory chemical used as a buffering agent and a source of phosphate ions. It is a white, crystalline solid that is soluble in water. The compound is commonly used in cell culture media and other biochemical applications to maintain a stable pH environment.
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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The Complete Protease Inhibitor Cocktail is a laboratory product designed to inhibit a broad spectrum of proteases. It is a concentrated solution containing a mixture of protease inhibitors effective against a variety of protease classes. This product is intended to be used in research applications to preserve the integrity of target proteins by preventing their degradation by proteolytic enzymes.
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The BCA Protein Assay Kit is a colorimetric detection and quantification method for total protein concentration. It utilizes bicinchoninic acid (BCA) for the colorimetric detection and quantification of total protein. The assay is based on the reduction of Cu2+ to Cu1+ by protein in an alkaline medium, with the chelation of BCA with the Cu1+ ion resulting in a purple-colored reaction product that exhibits a strong absorbance at 562 nm, which is proportional to the amount of protein present in the sample.
More about "Sodium glycerophosphate"
Sodium glycerophosphate, also known as sodium glycerol phosphate or sodium 2,3-dihydroxypropyl phosphate, is a water-soluble salt derived from glycerophosphoric acid and sodium.
This compound has a wide range of applications in the pharmaceutical and biomedical fields.
In cell culture media, sodium glycerophosphate serves as a buffer, helping to maintain the optimal pH and ionic balance.
It is also used as a source of organic phosphate, which is important for bone and tissue regeneration processes.
Researchers have explored the potential neuroprotective and anti-inflammatory properties of sodium glycerophosphate, making it a subject of interest in various therapeutic areas.
Dexamethasone, a synthetic glucocorticoid, is often used in combination with sodium glycerophosphate and β-glycerophosphate (another related compound) to stimulate osteogenic differentiation and mineralization in cell culture models.
Protease inhibitor cocktails, which contain a mixture of compounds designed to inhibit various proteases, can also be utilized alongside sodium glycerophosphate to maintain the integrity of proteins during experimental procedures.
Ascorbic acid, also known as vitamin C, is another important component that can be used in conjunction with sodium glycerophosphate, as it plays a crucial role in collagen synthesis and extracellular matrix formation.
PVDF (polyvinylidene fluoride) membranes are often employed in Western blot analyses to detect and quantify proteins, and sodium β-glycerophosphate may be used as a substrate in these assays.
Fetal bovine serum (FBS) is a commonly used supplement in cell culture media, and it can be combined with sodium glycerophosphate to support the growth and differentiation of various cell types.
Complete protease inhibitor cocktails, which contain a broad spectrum of protease inhibitors, can also be utilized to protect proteins from degradation in experiments involving sodium glycerophosphate.
To enhance the reproducibility and accuracy of your studies, you can explore protocols and products related to sodium glycerophosphate using the AI-powered search and comparison tools provided by PubCompare.ai.
This platform can help you identify the best protocols and products for your research, ultimately improving the quality and reliability of your findings.
This compound has a wide range of applications in the pharmaceutical and biomedical fields.
In cell culture media, sodium glycerophosphate serves as a buffer, helping to maintain the optimal pH and ionic balance.
It is also used as a source of organic phosphate, which is important for bone and tissue regeneration processes.
Researchers have explored the potential neuroprotective and anti-inflammatory properties of sodium glycerophosphate, making it a subject of interest in various therapeutic areas.
Dexamethasone, a synthetic glucocorticoid, is often used in combination with sodium glycerophosphate and β-glycerophosphate (another related compound) to stimulate osteogenic differentiation and mineralization in cell culture models.
Protease inhibitor cocktails, which contain a mixture of compounds designed to inhibit various proteases, can also be utilized alongside sodium glycerophosphate to maintain the integrity of proteins during experimental procedures.
Ascorbic acid, also known as vitamin C, is another important component that can be used in conjunction with sodium glycerophosphate, as it plays a crucial role in collagen synthesis and extracellular matrix formation.
PVDF (polyvinylidene fluoride) membranes are often employed in Western blot analyses to detect and quantify proteins, and sodium β-glycerophosphate may be used as a substrate in these assays.
Fetal bovine serum (FBS) is a commonly used supplement in cell culture media, and it can be combined with sodium glycerophosphate to support the growth and differentiation of various cell types.
Complete protease inhibitor cocktails, which contain a broad spectrum of protease inhibitors, can also be utilized to protect proteins from degradation in experiments involving sodium glycerophosphate.
To enhance the reproducibility and accuracy of your studies, you can explore protocols and products related to sodium glycerophosphate using the AI-powered search and comparison tools provided by PubCompare.ai.
This platform can help you identify the best protocols and products for your research, ultimately improving the quality and reliability of your findings.