2 5 dihydrobenzoic acid

Manufactured by Merck Group

Sourced in United States

2,5-dihydrobenzoic acid is a chemical compound used in various laboratory applications. It is a white crystalline solid with the molecular formula C₇H₆O₃. The compound serves as a precursor for the synthesis of other organic compounds, but a detailed description of its core function is not available while maintaining an unbiased and factual approach.

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Lab products found in correlation

Ultraflex 2 tof tof system, by Bruker (2 mentions) N isopropylacrylamide nipam, by Merck Group (1 mentions) Hydroquinone, by Merck Group (1 mentions) 2 2 azobisisobutyronitrile, by Merck Group (1 mentions) 2 hydroxyethyl methacrylate hema, by Merck Group (1 mentions) Acetonitrile, by Merck Group (1 mentions) Acetic acid, by Merck Group (1 mentions) Diethyl ether, by Merck Group (1 mentions) Acetonitrile acn, by Merck Group (1 mentions)

4 protocols using 2 5 dihydrobenzoic acid

Permethylation and MALDI-TOF Analysis of Glycans

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Dried samples were permethylated by standard procedures³⁹. Two hundred μl NaOH/DMSO slurry was added to samples followed by 200 μl methyl iodide. Samples were shaken for 30 minutes and then spun down at 5000 × g for 5 minutes. Supernatant was collected and chloroform extraction performed to isolate permethylated glycans. Five hundred μl chloroform and 500 μl water were added to supernatant, mixed, and centrifuged 5000 × g for 1 minute. Two more washes with 500 μl water were performed before evaporating chloroform by centrivap for 30 minutes. Bn-O-glycans were then resuspended in 25 or 50 μl 50% methanol. 0.5 μl matrix (10 mg/ml 2,5-dihydrobenzoic acid (Sigma), 50% acetonitrile, 0.1% TFA) and 0.5 μl sample were spotted on an Anchorchip target plate, air dried, and analyzed by MALDI-TOF mass spectrometry using Ultraflex-II TOF-TOF system (Bruker Daltonics). Peak masses were identified and structures assigned by composition and knowledge of glycan biosynthetic pathways, or MS/MS where indicated. This procedure only detects non-sulfated/phosphorylated structures; however, these modifications have not been previously reported from cells in our study.

Kudelka M.R., Antonopoulos A., Wang Y., Duong D.M., Song X., Seyfried N.T., Dell A., Haslam S.M., Cummings R.D, & Ju T. (2015). Cellular O-Glycome Reporter/Amplification to Explore O-Glycans of Living Cells. Nature methods, 13(1), 81-86.

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Permethylation and MALDI-TOF Analysis

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Dried samples were permethylated by standard procedures³⁹. Two hundred µl NaOH/DMSO slurry was added to samples followed by 200 µl methyl iodide. Samples were shaken for 30 minutes and then spun down at 5000 × g for 5 minutes. Supernatant was collected and chloroform extraction performed to isolate permethylated glycans. Five hundred µl chloroform and 500 µl water were added to supernatant, mixed, and centrifuged 5000 × g for 1 minute. Two more washes with 500 µl water were performed before evaporating chloroform by centrivap for 30 minutes. Bn-O-glycans were then resuspended in 25 or 50 µl 50% methanol. 0.5 µl matrix (10 mg/ml 2,5-dihydrobenzoic acid (Sigma), 50% acetonitrile, 0.1% TFA) and 0.5 µl sample were spotted on an Anchorchip target plate, air dried, and analyzed by MALDI-TOF mass spectrometry using Ultraflex-II TOF-TOF system (Bruker Daltonics). Peak masses were identified and structures assigned by composition and knowledge of glycan biosynthetic pathways, or MS/MS where indicated. This procedure only detects non-sulfated/phosphorylated structures; however, these modifications have not been previously reported from cells in our study.

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Synthesis and Characterization of Responsive Hydrogels

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Sodium acetate (molecular
biology grade), acetic acid, diethyl ether (anhydrous, ≥99.7%,
with 1 ppm BHT as inhibitor), hydroquinone (HQ, ≥99%), acetonitrile
(ACN, ≥99.9%, HPLC gradient grade), 2,5-dihydrobenzoic acid
(DHB), N-isopropylacrylamide (NIPAm), deuterated
water (D₂O), 2,2′-azobis(isobutyronitrile) (AIBN),
potassium persulfate (KPS), and N,N,N′,N′-tetramethylethylenediamine (TEMED), HPLC grade
ethanol, 2,2′-azobis(isobutyronitrile) (AIBN), diethyl ether,
2-hydroxyethyl methacrylate (HEMA) 97% containing 200 ppm hydroquinone
(HQ) were all obtained from Sigma-Aldrich (St. Louis, MO, USA). Low-viscosity
locust bean gum (LBG, >94% (dry weight basis)) was supplied by
Megazyme
(Bray, Ireland) (LOT 150901a) (galactose:mannose ratio, 24:76). All
chemicals were used as received except for HEMA, which was passed
through an alumina column prior to polymerization to remove the inhibitor.^{18 (link)}

Arcos-Hernandez M., Naidjonoka P., Butler S.J., Nylander T., Stålbrand H, & Jannasch P. (2021). Thermoresponsive Glycopolymers Based on Enzymatically Synthesized Oligo-β-Mannosyl Ethyl Methacrylates and N-Isopropylacrylamide. Biomacromolecules, 22(6), 2338-2351.

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Phosphopeptide Enrichment Using TiO2

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Acetonitrile (ACN) (Sigma Aldrich, St Louis, USA) at a final concentration of 30% was added to the tryptic peptides and the pH was adjusted to 2. Ten milligram of Titasphere TiO2 beads (MZ Analysentechnik, Mainz, Germany) in loading buffer [30 mg/ml 2,5 dihydrobenzoic acid (Sigma Aldrich, St Louis, USA), 80% ACN] were added to the sample and incubated at room temperature with rotation for 1 h. The beads were pelleted and the decanted supernatant was further incubated with a fresh batch of 5 mg of beads for 30 min. This step was repeated one further time, giving three fractions of enriched phosphoproteins bound to beads in total. Phosphopeptides bound to the beads were washed vigorously with shaking for 10 min in 1 ml of wash buffer 1 (30% acetonitrile, 3% trifluoroacetic acid) followed by an additional 10 min of vigorous wash with wash buffer 2 (80% acetonitrile, 0.1% trifluoroacetic acid). Phosphopeptides were loaded onto C8 stage tip, washed with wash buffer 2 and then eluted with 3 × 50 μl Elution buffer [40% Mass-spec grade NH₄OH (aq, 25% NH₃; Sigma-Aldrich, St Louis, USA), 60% acetonitrile (pH 10.5 or higher)]. Solvent was removed in a speed drying vacuum at room temperature and peptides were resuspended in 20 μl Solvent A (2% ACN, 0.1% formic acid).

Nakedi K.C., Nel A.J., Garnett S., Blackburn J.M, & Soares N.C. (2015). Comparative Ser/Thr/Tyr phosphoproteomics between two mycobacterial species: the fast growing Mycobacterium smegmatis and the slow growing Mycobacterium bovis BCG. Frontiers in Microbiology, 6, 237.

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