Dextran sulfate

Manufactured by Merck Group

Sourced in United States, Germany, Belgium, Macao

Dextran sulfate is a polysaccharide derived from the fermentation of sucrose. It is a high-molecular-weight anionic compound commonly used in laboratory research as a precipitation agent and for the separation of biomolecules.

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Lab products found in correlation

Formamide, by Merck Group (17 mentions) Formamide, by Thermo Fisher Scientific (9 mentions) Yeast trna, by Thermo Fisher Scientific (6 mentions) Chondroitin sulfate, by Merck Group (5 mentions) Heparin, by Merck Group (5 mentions) Ribonucleoside vanadyl complex, by New England Biolabs (5 mentions) Yeast trna, by Merck Group (5 mentions) Bovine serum albumin (bsa), by Merck Group (5 mentions) Chitosan, by Merck Group (3 mentions) Deionized formamide, by Thermo Fisher Scientific (3 mentions) Superase in rnase inhibitor, by Thermo Fisher Scientific (3 mentions) Mgcl2, by Merck Group (3 mentions) Lsm 710 confocal microscope, by Zeiss (3 mentions) Rnase free bsa, by Thermo Fisher Scientific (3 mentions) Lsm 900 confocal microscope, by Zeiss (3 mentions) Oligoarray complex pools, by Twist Bioscience (2 mentions) Qlaquick pcr purification kit, by Qiagen (2 mentions) Ep7051, by Thermo Fisher Scientific (2 mentions) Polyethyleneimine, by Merck Group (2 mentions) L ascorbic acid, by Thermo Fisher Scientific (2 mentions)

Spelling variants of this product

DSS (216 citations) Dextrans (38 citations) Dextran sulfate sodium salt (35 citations) Dextran sulfate sodium salt (DSS, (9 citations) Dextran-sulfate (DS; (7 citations) Sodium dextran sulfate (5 citations) DEAE-dextran sulfate (3 citations) Dextran sulfate sodium salt from Leuconostoc spp. (2 citations)

109 protocols using dextran sulfate

Macrophage Oxidative Stress Assay

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Reduced-glutathione (GSH), citric acid, phosphoric acid, lipopolysaccharides (LPS), sulfanilamide, dichlorofluorescein diacetate (DCFDA), N-1-napthylethylenediamine dihydrochloride, dextran sulfate, sodium azide and dextran sulfate were purchased from Sigma-Aldrich (St. Louis, MO).
Mouse macrophage cell line (Raw264.7), Dulbecco’s modified eagle’s medium (DMEM) (30–2601) and penicillin-streptomycin solution (30–2300) were purchased from ATCC (Manassas, VA). Fetal bovine serum (FBS) was purchased from Atlantic biological (Atlanta, GA). All other reagents and solvents were of analytical grade.

Oh B., Lee Y., Fu M, & Lee C.H. (2017). Computational Analysis on Down-Regulated Images of Macrophage Scavenger Receptor. Pharmaceutical research, 34(10), 2066-2074.

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Fabrication of Bioactive PLGA Nanoparticles

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PLGA with an inherent viscosity (i.v.) of 0.57 dLg ⁻¹ (50:50, PLGA DL LOW IV, lot # A11-071, lauryl ester end group, 51 kDa) was purchased from Lakeshore Biomaterials (Birmingham, Alabama). High molecular weight (~ 500 kDa) dextran sulfate (HDS), low molecular weight (~15.5 kDa) dextran sulfate (LDS), chondroitin sulfate (~ 63 kDa, shark cartilage) (CS), porcine heparin (~18 kDa) (HP) sodium salts were purchased from Sigma-Aldrich. Chitosan (~ 61 kDa) was also from Sigma-Aldrich. Sodium hyaluronate (HA) powders and VEGF165 were obtained as a gift from Lifecore Biomedical (MN, USA) and Genentech, respectively. Lysozyme (chicken egg white) and magnesium carbonate were purchased from Sigma-Aldrich. FgF-20 was obtained from the National Cancer Institute-Biometric Research Branch (NCI-BRB) preclinical repository. Human VEGF standard ELISA development kit was purchased from Peprotech (NJ, USA). Cyanine-5 labelled lysozyme was bought from Nanocs (NY, USA). All other reagents, common solvents, and supplies were obtained from Sigma-Aldrich, unless otherwise specified.

Shah R.B, & Schwendeman S.P. (2014). A Biomimetic Approach to Active Self-Microencapsulation of Proteins in PLGA. Journal of controlled release : official journal of the Controlled Release Society, 0, 60-70.

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Telomere FISH Protocol for Cell Cultures

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The cells cultured on glass coverslips were fixed in 4% paraformaldehyde and permeabilized with 0.2% Triton X-100, followed by washing with 2 × SSC and then incubated at 57°C for 30 min in prehybridization solution containing 40% formamide (Wako), 2 × SSC, 0.8 mg/mL tRNA (Roche), 0.8 mg/mL single strand salmon sperm DNA (Sigma-Aldrich), 0.16% BSA, 8% Dextran sulfate (Sigma-Aldrich), 1.6 mM Ribonucleoside-vanadyl complex (New England Biolabs) and 5 mM EDTA. Then the coverslips were incubated at 57°C overnight in hybridization solution containing 40% formamide (Wako), 2 × SSC, 0.8 mg/mL tRNA (Roche), 0.8 mg/mL single strand salmon sperm DNA (Sigma-Aldrich), 0.16% BSA, 8% Dextran sulfate (Sigma-Aldrich), 1.6 mM Ribonucleoside-vanadyl complex (New England Biolabs), 5 mM EDTA, 20 ng (HeLa) or 10 ng (fibroblast)/mL 5′ Cy3-labeled (C₄G₂) × 4 probe (IDT).³⁹ (link) The following day, cells were washed three times for 30 min each at 57°C with 40% formamide (Wako), 0.5 × SSC, and then with 0.5 × SSC for 10 min each at room temperature. After a brief rinsing with PBS, nuclei were stained with 0.1 μg/mL DAPI for 20 min and then washed three times with 0.02% Tween in PBS for 5 min each. Glass coverslips were mounted with ProLong Diamond Antifade (Life Technologies). Fluorescence images were obtained using a Confocal Laser Scanning Microscope LSM710 (Carl Zeiss).

Uozumi R., Mori K., Gotoh S., Miyamoto T., Kondo S., Yamashita T., Kawabe Y., Tagami S., Akamine S, & Ikeda M. (2024). PABPC1 mediates degradation of C9orf72-FTLD/ALS GGGGCC repeat RNA. iScience, 27(3), 109303.

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Whole-mount RNA in situ Hybridizations

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Whole-mount chromogenic RNA in situ hybridizations were performed as previously described (Gamse et al., 2003 (link)). Whole-mount fluorescence RNA in situ hybridizations were performed as previously described with the addition of 5% dextran sulfate (Sigma) to enhance the staining (Lauter et al., 2011 (link)). Information on RNA probes is listed in Table S2. For detailed protocols, see supplementary Materials and Methods.

Khuansuwan S., Clanton J.A., Dean B.J., Patton J.G, & Gamse J.T. (2016). A transcription factor network controls cell migration and fate decisions in the developing zebrafish pineal complex. Development (Cambridge, England), 143(14), 2641-2650.

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SCARA5 Interactions with VWF and FVIII

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The interaction between recombinant SCARA5 and VWF/FVIII was measured as described [15 (link)] with several modifications. Recombinant human SCARA5 was coated in carbonate buffer at 5 μg/mL on Maxisorp plates (Nunc, Rochester, USA). VWF binding to SCARA5 was detected by an HRP-conjugated rabbit anti-VWF antibody (Dako, Agilent, Santa Clara, USA), FVIII binding to SCARA5 was detected by an HRP-conjugated sheep anti-FVIII antibody (Affinity Biologicals, Ancaster, Canada). For all experiments, binding was compared with background binding to a BSA-coated negative control. For some experiments, immobilized SCARA5 was preincubated with polyinosinic acid potassium salt (PolyI), poly guanylic acid (PolyG), dextran sulfate, chondroitin sulfate (Sigma Aldrich, St. Louis, USA), polyphosphate (PolyP) (courtesy of Dr. JH Morrissey, University of Michigan), or the following anti-SCARA5 antibodies: PA5–23551 (Invitrogen), LS-B5013 (LS Bio), AF4900 (R&D), or mouse anti-human SCARA5 αh-SR5.2. αh-SR5.2 was produced and purified as previously described [18 (link)] using a human SCARA5 peptide (amino acids 356–495) in an pET28a(+) vector. Antibody binding sites can be found in Supplemental Figure 2.

Swystun L.L., Ogiwara K., Lai J.D., Ojala J.R., Rawley O., Lassalle F., Notley C., Rengby O., Michels A., Nesbitt K., Tryggvason K, & Lillicrap D. (2019). The scavenger receptor SCARA5 is an endocytic receptor for von Willebrand factor expressed by littoral cells in the human spleen. Journal of thrombosis and haemostasis : JTH, 17(8), 1384-1396.

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Small RNA FISH in Drosophila Testes

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smRNA-FISH was conducted as described^{61 (link)}. Testes from 2–3-day-old flies were dissected in 1× PBS, fixed in 4% formaldehyde in 1× PBS for 30 min, washed in PBS and permeabilized in 70% ethanol overnight at 4 °C. The following day, testes were rinsed with wash buffer (2× saline-sodium citrate and 10% formamide) and hybridized overnight at 37 °C in hybridization buffer (2× saline-sodium citrate, 10% dextran sulfate (Sigma, D8906), 1 mg ml⁻¹Escherichia coli tRNA (Sigma, R8759), 2 mM vanadyl ribonucleoside complex (NEB, S142), 0.5% bovine serum albumin (Ambion, AM2618) and 10% formamide). Following hybridization, samples were washed three times in wash buffer for 20 min each at 37 °C and mounted in VECTASHIELD with 4′,6-diamidino-2-phenylindole (DAPI, Vector Labs). Fluorescently labelled probes were added to the hybridization buffer to a final concentration of 100 nM. DNA oligo probes to detect Ste and Su(Ste) RNA were conjugated with Quasar 570, Cy3 or Cy5 fluorophores (Biosearch Technologies and IDT; for probe information, see Supplementary Table 5). Images were acquired using an upright Leica TCS SP8 confocal microscope with a 63× oil immersion objective lens (numerical aperture 1.4) and processed using ImageJ.

Venkei Z.G., Gainetdinov I., Bagci A., Starostik M.R., Choi C.P., Fingerhut J.M., Chen P., Balsara C., Whitfield T.W., Bell G.W., Feng S., Jacobsen S.E., Aravin A.A., Kim J.K., Zamore P.D, & Yamashita Y.M. (2023). A maternally programmed intergenerational mechanism enables male offspring to make piRNAs from Y-linked precursor RNAs in Drosophila. Nature Cell Biology, 25(10), 1495-1505.

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Oligoarray-based DNA Probe Synthesis

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Primary probes were ordered as an oligoarray complex pools from Twist Bioscience and were constructed as previously described ^{6 (link),11 (link),21}. Briefly, a 2-step limited PCR cycles were used to amplify the designated probe sequences from the oligo complex tool. Then, the amplified products were purified using QlAquick PCR Purification Kit (28104; Qiagen) according to the manufacturer's instructions. The PCR products were used as the template for in vitro transcription (E2040S; NEB) followed by reverse transcription (EP7051; Thermo Fischer) with the forward primer. After alkaline hydrolysis, the single stranded DNA (ssDNA) probes were purified by ethanol precipitation and resuspend in primary probe hybridization buffer comprising of 30% formamide (F9037; Sigma), 2× SSC (15557036; Thermo Fischer), and 10% (w/v) Dextran Sulfate (D8906; Sigma). The probes were stored at -20°C.

Eng C.H., Shah S., Thomassie J, & Cai L. (2017). Profiling the transcriptome by RNA SPOTs. Nature methods, 14(12), 1153-1155.

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Quantification of FXII and PK Activation

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Materials used were as follows: normal human plasma (Precision BioLogic, Dartmouth, Canada); FXII-deficient plasma (George King Biomed); FXII, FXIIa, βFXIIa, PK, PKa, α-thrombin, corn trypsin inhibitor, and horseradish peroxidase–conjugated goat anti-human FXII and anti-human PK (Enzyme Research Laboratory, South Bend, IN); dextran sulfate (500 000 Da), polyethyleneimine (PEI; 750 000 Da), soybean trypsin inhibitor, and ε-aminocaproic acid (ε-ACA; Sigma-Aldrich, St. Louis, MO); ellagic acid (ACROS Organics, The Hague, Netherlands); S2302 (H-d-prolyl-l-phenylalanyl-l-arginine-p-nitroanilide) and S-2366 (l-pyro-Glu-l-Pro-l-Arg-p-nitroanilide; DiaPharma, Westchester, OH); PTT-A reagent (Diagnostica Stago, Asnieres-sur-Seine, France); argatroban (GlaxoSmithKline, Brentford, United Kingdom); polyphosphate (poly-P; 200-1300 units; provided by James Morrissey, University of Michigan); and horseradish peroxidase–conjugated antihemagglutinin immunoglobulin G (IgG; Invitrogen). Monoclonal IgGs 15H8 and 1B2^{8,18 (link)} are described.

Shamanaev A., Ivanov I., Sun M.F., Litvak M., Srivastava P., Mohammed B.M., Shaban R., Maddur A., Verhamme I.M., McCarty O.J., Law R.H, & Gailani D. (2022). Model for surface-dependent factor XII activation: the roles of factor XII heavy chain domains. Blood Advances, 6(10), 3142-3154.

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Pancreatic Ductal Adenocarcinoma Cell Lines

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We used 10 PDAC cell lines, AsPC-1, BxPC-3, Capan-2, CFPAC-1, MIAPaCa-2, PANC-1, SW1990 (American Type Culture Collection, Manassas, VA, USA), KP-2, KP-3 (JCRB Cell Bank, Osaka, Japan), and NORP-1 (RIKEN BRC Cell Bank, Tsukuba, Ibaraki, Japan). An immortalized cell line derived from human pancreatic duct, HPDE, was a kind gift from Dr. M.S. Tsao (Dept. of Pathology, Univ. of Toronto, Canada). PDAC cell lines were maintained in RPMI1640 medium (Life Technologies, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (FBS) (Life Technologies) and 1% streptomycin and penicillin (Life Technologies). HPDE was maintained in HuMedia-KG2 (KURABO, Osaka, Japan), in a 5% CO² incubator at 37° C. 4-Methylumbelliferone (4-MU) and dextran sulfate were purchased from SIGMA-ALDRICH Corp. (St. Louis, MO, USA).

Kudo Y., Kohi S., Hirata K., Goggins M, & Sato N. (2019). Hyaluronan activated-metabolism phenotype (HAMP) in pancreatic ductal adenocarcinoma. Oncotarget, 10(54), 5592-5604.

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Visualization of NEAT1 Long Isoform in HeLa Cells

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HeLa^GFP-NONO cells, uninduced or expressing GFP-NONO, were seeded at approximately 70% confluency on the day prior to fixation, then fixed for 10 min in 4% paraformaldehyde (in PBS), and washed once with PBS. Cells were permeabilized in 70% ethanol for at least 1 h at 4 °C and washed once with wash buffer for 5 min. Wash buffer was prepared with 10% formamide (Ambion) in 2× SSC (contains 0.3 M of NaCl and 30 mM of sodium citrate). Hybridization buffer was prepared with 100 mg/ml dextran sulfate (Sigma) and 10% formamide in 2× SSC. A hybridization mixture was prepared using 125 nM of Stellaris FISH Probes (Biosearch Technologies, Inc) targeted to the long isoform of human NEAT1 labeled with Quasar 570 Dye (SMF-2037-1, Biosearch), made to a final concentration of 100 mg/ml dextran sulfate, 10% formamide, and 2× SSC. Each coverslip was transferred onto a 50 μl drop of hybridization mixture, cells side down, incubated in a sealed, dark humidified chamber overnight at 37 °C. Coverslips were then rinsed with wash buffer for 30 min at 37 °C in the dark, counterstained with DAPI (5 ng/ml in wash buffer) for 30 min at 37 °C in the dark, and finally rinsed in 2× SSC. Coverslips were mounted onto microscopic slides using Vectashield mounting medium.

Lee P.W., Marshall A.C., Knott G.J., Kobelke S., Martelotto L., Cho E., McMillan P.J., Lee M., Bond C.S, & Fox A.H. (2022). Paraspeckle subnuclear bodies depend on dynamic heterodimerisation of DBHS RNA-binding proteins via their structured domains. The Journal of Biological Chemistry, 298(11), 102563.

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