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Sulfatases

Sulfatases are a class of enzymes that catalyze the hydrolysis of sulfate esters, playing a crucial role in the metabolism and regulation of sulfated biomolecules.
These enzymes are involved in diverse biological processes, including the degradation of glycosaminoglycans, the desulfation of steroid hormones, and the modulation of signaling pathways.
Sulfatases are found in a wide range of organisms, from bacteria to humans, and their dysregulation has been implicated in various diseases, such as lysosomal storage disorders and cancers.
Understandinng the structure, function, and regulation of sulfatases is an active area of research, with implications for developing targeted therapies and improving our knowledge of sulfate-dependent biological systems.
PubCompare.ai's AI-driven protocol comparision can help researchers optimize their sulfatase studies, ensuring improved reproducibility and accuracy through the identification of the most effective research methods from literature, preprints, and patents.

Most cited protocols related to «Sulfatases»

Sulfatase Sequence Identification and Analysis

Cited 23 times

Sulfatase sequences were extracted from the UniProt database in August 2009 using the BlastP program [70 (link)]. Alkylsulfohydrolases (370 proteins) and arylsulfohydrolases (15 proteins), which belong to the metallo-β-lactamase superfamily, were identified by at least 30% sequence identity over ~600 residues with the characterized enzymes alkylsulfatase SdsA1 (Uniprot code: Q9I5I9) and arylsulfatase AtsA (P28607), respectively, and by the presence of the pattern HxHxDH, which is involved in the coordination of two catalytic zinc ions. Fe αKG-dependent alkylsulfodioxygenases (111 proteins) were identified by at least 30% sequence identity over ~300 residues with the characterized alkylsulfodioxygenase AtsK (Q9WWU5) and by the presence of the pattern HxD/Ex_nH (n = 39 to 154) involved in the coordination of the Fe ion [23 (link)]. The extracted sulfatase sequences were subjected to multiple sequence alignments using the MAFFT [71 (link)] program, with the iterative refinement method L-INS-i and the scoring matrix Blosum62. Complete sets of orthologous alkysulfohydrolases and arylsulfohydrolases on one hand, and alkylsulfodioxygenases on the other hand, were classified based on phylogenetic analyzes using the metallo-β-lactamases and Fe αKG-dependent dioxygenase superfamilies, respectively.
The identification of FGly-sulfatases (4058 proteins) was based on a significant level of sequence identity of at least 25% with characterized enzymes (Table 1) over a minimal length compatible with the size of the known FGly-sulfatases (at least 400 residues), and by the conservation of the two PROSITE signatures PS00523 and PS00149 which correspond to the simplified patterns [SAPG]-[LIVMST]-[CS]-[STACG]-P-[STA]-R-x(2)-[LIVMFW](2)-[TAR]-G and G-[YV]-x-[ST]-x(2)-[IVAS]-G-K-x(0,1)-[FYWMK]-[HL], respectively [30 (link), 31 (link)]. The proteins encompassing several FGly-sulfatase modules were divided into distinct sequences corresponding to each catalytic module. Due to the huge number of sequences, it is impossible to directly obtain a reliable multiple alignment of this large group of sequences. Therefore, the FGly-sulfatase sequences were first divided into 81 groups and 32 orphan sequences, on the basis of sequence identities using the BlastP program. A multiple sequence alignment was obtained for each of these groups using MAFFT [71 (link)] with the iterative refinement method L-INS-i and the scoring matrix Blosum62. Then these 81 multiple sequence alignments were manually stacked on each other by matching similar zones using Jalview [72 (link)]. The alignments were manually improved using Jalview on the basis of the sequence alignment derived from the superposition of available crystal structures of sulfatases (Table 1). After this refinement step, the poorly conserved regions were removed from the multiple sequence alignment. The different phylogenetic trees were derived from these refined alignments using Maximum Likelihood method with the program RAxML with the MTMAMF or WAG as substitution matrix [73 (link)] or with the program MEGA 5.2.2 [74 (link)]. The reliability of the trees was always tested by bootstrap analysis using 100 resamplings of the dataset. The trees were displayed with MEGA 5.2.2 [74 (link)]. For the FGly-sulfatase sequences, the program MatGat [75 (link)] was used and two identity matrices were generated, one for the full length proteins and the second matrix corresponding to the edited multiple sequence alignment. The logo sequences were built using WebLogo via the PROSITE databank [76 (link)].

Barbeyron T., Brillet-Guéguen L., Carré W., Carrière C., Caron C., Czjzek M., Hoebeke M, & Michel G. (2016). Matching the Diversity of Sulfated Biomolecules: Creation of a Classification Database for Sulfatases Reflecting Their Substrate Specificity. PLoS ONE, 11(10), e0164846.

Publication 2016

alkylsulfatase beta-Lactamase Catalysis Dioxygenases Enzymes Isovaleryl-CoA Dehydrogenase Deficiency Orphaned Children Proteins Sequence Alignment Sulfatases Trees Zinc

Quantifying PAH Metabolites in Urine

Cited 14 times

All solvents were HPLC grade, and chemicals were reagent grade. We
purchased acetonitrile, ethanol, 0.1% formic acid in water, methanol,
water, and ammonium fluoride from Thermo Fisher Scientific (Waltham, MA, USA);
ascorbic acid, sodium acetate, and Helix pomatia β-glucuronidase type
H-1 (β-glucuronidase ≥300,000 units/g, sulfatase ≥10,000
units/g) from Sigma-Aldrich (St. Louis, MO, USA). We obtained
1-hydroxynaphthalene (1-OH-NAP), 2-hydroxynaphthalene (2-OH-NAP),
2-hydroxyfluorene (2-OH-FLU), 3-hydroxyfluorene (3-OH-FLU),
1-hydroxyphenanthrene (1-OH-PHE), 2-hydroxyphenanthrene, 3-hydroxyphenanthrene,
4-hydroxyphenanthrene (4-OH-PHE), 1-hydroxypyrene (1-OH-PYR), and their
corresponding ¹³C-labeled internal standards (IS, listed in Table 1) from Cambridge Isotope
Laboratories (Andover, MA, USA).
We purchased smokers’ urine samples from BioreclamationIVT
(Westbury, NY, USA). We also collected urine anonymously in 2015 from non-smoker
adult volunteers with no documented occupational exposure to PAHs in Atlanta,
GA. We obtained two Standard Reference Materials® (SRMs), SRM 3672
(smoker urine) and SRM 3673 (non-smoker urine), from the US National Institute
of Standards and Technology (NIST) (Gaithersburg, MD, USA). All urine specimens
were stored upon collection or arrival at −70 °C until use.
Appropriate safety control measures (including engineering,
administrative, and personal protective equipment) were used for all procedures
based on a site-specific risk assessment that identified physical, health, and
procedural hazards.

Wang Y., Meng L., Pittman E.N., Etheredge A., Hubbard K., Trinidad D.A., Kato K., Ye X, & Calafat A.M. (2016). Quantification of Urinary Mono-hydroxylated Metabolites of Polycyclic Aromatic Hydrocarbons by on-line Solid Phase Extraction-High Performance Liquid Chromatography-Tandem Mass Spectrometry. Analytical and bioanalytical chemistry, 409(4), 931-937.

Publication 2016

1-hydroxyphenanthrene 1-hydroxypyrene 1-nitro-2-acetylpyrrole 2-hydroxyfluorene 2-naphthol 4-hydroxyphenanthrene acetonitrile ammonium fluoride Ascorbic Acid beta-Glucuronidase Ethanol formic acid Health Risk Assessment Helix (Snails) High-Performance Liquid Chromatographies Methanol N-(2-naphthalenesulfonyl)aspartyl-(2-phenethyl)amide Naphthols Non-Smokers Occupational Exposure Physical Examination Polycyclic Hydrocarbons, Aromatic Safety Sodium Acetate Solvents Sulfatases Urine Voluntary Workers

Quantification of Glucosinolates in Freeze-Dried Samples

Cited 11 times

Glucosinolates were extracted and analyzed as previously described.^{16,17 (link)} Freeze-dried samples (100 mg) were boiled in 5 mL water for 10 min. The supernatant was collected after centrifugation (5 min, 4000g), and the residues were washed once with water (5 mL), centrifuged and then combined with the previous extract. The aqueous extract was applied to a DEAE-Sephadex A-25 (40 mg) column (pyridine acetate form) (GE Healthcare, Piscataway, NJ). The glucosinolates were converted into their desulpho analogues by overnight treatment with 100 μL of 0.1% (1.4 units) aryl sulphatase (Sigma), and the desulphoglucosinolates were eluted with 2 × 0.5 mL water. HPLC analysis of desulphoglucosinolates was carried out using a Waters High-performance Liquid Chromatography (HPLC) instrument equipped with a Model 2996 PDA absorbance detector (Waters, USA). Samples (20 μL) were separated at 30 °C on a Waters Spherisorb C18 column (250 × 4.6 mm i.d.; 5 μm particle size) using acetonitrile and water at a flow rate of 1.0 mL min⁻¹. Absorbance was detected at 226 nm. ortho-Nitrophenyl-β-d-galactopyranoside (Sigma) was used as an internal standard for HPLC analysis.

Sun B., Tian Y.X., Jiang M., Yuan Q., Chen Q., Zhang Y., Luo Y., Zhang F, & Tang H.R. (2018). Variation in the main health-promoting compounds and antioxidant activity of whole and individual edible parts of baby mustard (Brassica juncea var. gemmifera). RSC Advances, 8(59), 33845-33854.

Publication 2018

Acetate acetonitrile Centrifugation DEAE Sephadex Freezing Galactose Glucosinolates High-Performance Liquid Chromatographies pyridine Sulfatases

Quantification of Pesticide Metabolites in Urine

Cited 10 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2018

Acetic Acid Acetone acetonitrile ARID1A protein, human beta-Glucuronidase Buffers Chromatography CREB3L1 protein, human Electrons Enzymes Hexanes High-Performance Liquid Chromatographies Mass Spectrometry Methanol Nitrogen Pesticides Sodium Acetate Solid Phase Extraction Sulfatases Tandem Mass Spectrometry Urine Vacuum

Pyrethroid Metabolite Analysis in Urine

Cited 9 times

The urine for pyrethroid measurements was aliquoted at the collection site, stored cold (2–4°C) or frozen until shipment to CDC’s National Center for Environmental Health laboratory on dry ice. Urinary creatinine concentrations were determined using an automated colorimetric method based on a modified Jaffe reaction (Jaffe 1886 ) on a Beckman Synchron AS/ASTRA clinical analyzer (Beckman Instruments, Inc., Brea, CA) at the Fairview University Medical Center (Minneapolis, MN). We analyzed urine samples for pyrethroid metabolites using established methodology (Baker et al. 2004 (link); Olsson et al. 2004 (link)). Briefly, 2 mL urine was spiked with an internal standard mixture consisting of isotopically labeled 3PBA and trans-DCCA and incubated with β-glucuronidase/sulfatase to liberate conjugated metabolites. The hydrolysates were extracted using OASIS HLB (Waters Corp., Milford, MA) mixed-mode solid-phase extraction cartridges. The cartridges were washed with 5% methanol in a 0.1% acetic acid solution, and the metabolites were eluted using methanol. The extracts were concentrated and analyzed using high-performance liquid chromatography/electrospray chemical ionization/tandem mass spectrometry. 3PBA and trans-DCCA were quantified using isotope dilution calibration, whereas 4F3PBA, cis-DCCA, and cis-DBCA were quantified using the labeled 3PBA, labeled trans-DCCA, and labeled trans-DCCA, respectively, as internal standards. Positive and negative control samples represented 10% of the samples analyzed to ensure proper method operation. Metabolite concentrations were adjusted using creatinine concentrations to correct for variable urine dilutions in the “spot” urine samples. Both laboratories and methods were certified according to guidelines set forth in the Clinical Laboratory Improvement Amendment of 1988 .

Barr D.B., Olsson A.O., Wong L.Y., Udunka S., Baker S.E., Whitehead RD J.r., Magsumbol M.S., Williams B.L, & Needham L.L. (2010). Urinary Concentrations of Metabolites of Pyrethroid Insecticides in the General U.S. Population: National Health and Nutrition Examination Survey 1999–2002. Environmental Health Perspectives, 118(6), 742-748.

Publication 2010

Acetic Acid beta-Glucuronidase Clinical Laboratory Services Cold Temperature Colorimetry Creatinine CREB3L1 protein, human Dry Ice Freezing High-Performance Liquid Chromatographies Isotopes Methanol Pyrethroids Solid Phase Extraction Spectrometry Sulfatases Technique, Dilution Urine

Most recents protocols related to «Sulfatases»

Quantification of Glucosinolates in Arabidopsis

Glucosinolates were analyzed from 2-week-old R-o-18 and brclf mutant in accordance with a previously described protocol (Nugroho et al., 2021 (link)). They were extracted from whole fresh tissue samples with 70% aqueous methanol (methanol:water 70:30, v:v) at 70°C for 10 min. The extract was centrifuged at 3000 × g for 20 min, and the supernatant was transferred into a column containing Sephadex A-25 (Sigma-Aldrich Inc., USA). The column was reacted with 11.25 units of purified sulfatase (Sigma-Aldrich Inc., USA) at 37°C to allow desulfation for 12 h. Desulfo-glucosinolates (DS-GSLs) were eluted from the column with 1.5 ml of deionized water and evaporated using a speed vacuum. DS-GSLs were re-dissolved with 1 ml of HPLC water and filtered with 0.45 μm PVDF membrane (Biofact, Korea). They were chromatographically separated on a C18 reverse phase column (Zorbax XDB-C18, 4.6 × 250 mm², 5 μm particle size, Agilent, USA) with a gradient system composed of water (Thermo Fisher Scientific, USA) and acetonitrile (Honeywell, USA) in the Dionex Ultimate 3000 ultra-high performance liquid chromatography (U-HPLC) systems (Thermo Fisher Scientific, USA). Samples (20 μL) of DS-GSLs were analyzed using a diode array detector at 229 nm. All DS-GSL peaks detected in this study were identified in accordance with a previous study (Nugroho et al., 2019 (link)). Each DS-GSL was independently quantified from three biological replicates based on sinigrin (Sigma-Aldrich Inc., USA) standard compounds (Brown et al., 2003 (link)). Data were presented as micromoles per gram dry weight (µmol/gr DW).

Nugroho A.B., Kim S., Lee S.W, & Kim D.H. (2023). Transcriptomic and epigenomic analyses revealed that polycomb repressive complex 2 regulates not only developmental but also stress responsive metabolism in Brassica rapa. Frontiers in Plant Science, 14, 1079218.

Publication 2023

acetonitrile Biopharmaceuticals Glucosinolates High-Performance Liquid Chromatographies Methanol polyvinylidene fluoride sephadex sinigrin Sulfatases Tissue, Membrane Tissues Vacuum

Measuring Leukocyte ARSA Activity

ARSA activity was estimated as mu/mg protein in leukocytes, using 4-nitrocatechol sulfate. In brief: 0.25 mM sodium pyrophosphate was utilized to inactivate arylsulfatase B(ARSB). Then, the amount of sulfate released was measured by the absorbance of free 4-nitrocatechol at 515 nm on a spectrophotometer (Beckmann Coulter, Brea, CA, USA), which is associated with sulfatase activity [17 ].

Ataei Z., Nouri Z., Tavakoli F., Pourreza M.R., Narrei S, & Tabatabaiefar M.A. (2023). Novel in-frame duplication variant characterization in late infantile metachromatic leukodystrophy using whole-exome sequencing and molecular dynamics simulation. PLOS ONE, 18(2), e0282304.

Publication 2023

4-nitrocatechol sulfate Arylsulfatase B Leukocytes nitrocatechol Proteins sodium pyrophosphate Sulfatases Sulfates, Inorganic

Enzymatic Digestion and Extraction of PHYTO Conjugates

The digestion of PHYTOs conjugates (glucuronides and sulfates) was performed with β-glucuronidase-aryl sulfatase from Helix pomatia (Roche, 10127698001), diluted (5 µL.mL⁻¹) in sodium acetate buffer 0.1 M, 0.14 M EDTA, 100 UI.mL⁻¹ penicillin G (SIGMA, P-3032), 0.1 mg.mL⁻¹ streptomycin (SIGMA, S-6501), pH 5. The extraction of aglycone compounds was then performed using acidified ethyl-acetate (500 µL HCl 38% per L of ethyl-acetate).
All salt reagents were from VWR-France. The protocol also involved thyroglobulin from swine (SIGMA, T1126), bovine serum albumin (EUROMEDEX, 04-100-812-C), and secondary antibody goat anti-rabbit IgG antibody-Amdex (SIGMA, RPN4301). The revelation steps required o-phenylenediamine dihydrochloride (OPD) (SIGMA, P1526). Stock solutions were prepared at 10 mg.mL⁻¹ in water and stored in black vials at −22 °C. Glassware in contact with unconjugated PHYTOs was coated with Sigmacote^® (SIGMA, SL2). The sample, washing, and assay buffers were phosphate-buffered saline 0.01 M, 0.9% NaCl, 0.2% Tween, and 1% DMSO, pH 7.3. To obtain the saturation and antibody buffers, 1.6 mg.L⁻¹ of bovine serum albumin was added to the latter. The revelation buffer was citrate-phosphate buffer 0.15 M, pH 5, with 0.05 mg of OPD.mL⁻¹. The stop solution was H₂SO₄ 4 M. The primary antibodies were selected according to previous works [23 (link),24 (link),25 (link)]. They were harvested if required to avoid undesired cross-reactions with the unwanted antigen.

Bensaada S., Raymond I., Pellegrin I., Viallard J.F, & Bennetau-Pelissero C. (2023). Validation of ELISAs for Isoflavones and Enterolactone for Phytoestrogen Intake Assessment in the French Population. Nutrients, 15(4), 967.

Publication 2023

1,2-diaminobenzene anti-IgG Antibodies Antigens beta-Glucuronidase Biological Assay Buffers Citrates Cross Reactions Digestion Edetic Acid ethyl acetate Glucuronides Goat Helix (Snails) Immunoglobulins Normal Saline Penicillin G Phosphates Pigs Rabbits Saline Solution Serum Albumin, Bovine Sodium Acetate Sodium Chloride Streptomycin Sulfatases Sulfates, Inorganic Sulfoxide, Dimethyl Thyroglobulin Tweens

Desulfoglucosinolate Extraction and Analysis

GSLs were extracted from different plant parts, as previously reported [38 (link)]. To inactivate the endogenous myrosinase, plant material was ground into a fine powder, and 100 mg were extracted for 5 min at 80 °C in 2 mL MeOH/H₂O (70:30 v/v). Each extract was loaded onto a mini-column containing 0.5 mL of GE Healthcare’s DEAE-Sephadex A-25 anion exchange resin and conditioning it with 25 mM acetate buffer (pH 5.6). Buffer solution was added to the column after it had been washed with 70% MeOH and 1 mL of ultrapure water to create the optimal desulfation conditions. Purified sulfatase in the amount of 20 µL (0.35 U/mL) was placed into each mini-column and allowed to stand for 18 h at room temperature. The desulfoGSLs were then eluted with 1.5 mL of ultra-pure H₂O, lyophilised and diluted to 1 mL. The samples were kept at −20 °C until UHPLC-DAD-MS/MS analysis.

Đulović A., Burčul F., Čikeš Čulić V., Rollin P, & Blažević I. (2023). Glucosinolates and Cytotoxic Activity of Collard Volatiles Obtained Using Microwave-Assisted Extraction. Molecules, 28(4), 1657.

Publication 2023

Acetate Anion Exchange Resins Buffers DEAE Sephadex Galactosialidosis myrosinase Plants Powder Sulfatases Tandem Mass Spectrometry

Collard Cultivation and Glucosinolate Analysis

Plant samples of collard (Brassica oleracea L. convar. acephala var. viridis, Figure S1) were cultivated in Split (43°30′26″ N, 16°31′35″ E) and collected in April 2021. The leaves were blue-green, fleshy, and rounded at the base, and they were located on thickened petioles that partially enclosed the stem. The stem was upright, reaching up to 150 cm in height, and had a well-branched spindly root. The flowers had four bright yellow oval petals that were arranged in a rectangular pattern. The specimen voucher was stored under number ZOKBOAc1. Sinigrin, DEAE-Sephadex A-25 (GE Healthcare), sulfatase (type H-1 from Helix pomatia), and 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) were purchased from Sigma-Aldrich (St. Louis, MO, USA); glucotropaeolin (11), progoitrin (24R), 4-hydroxyglucobrassicin (28), glucobrassicin (43), neoglucobrassicin (47), 4-methoxyglucobrassicin (48), glucoraphanin (64), glucoerucin (84), and gluconasturtiin (105) were purchased from Phytoplan Diehm & Neuberger GmbH (Heidelberg, Germany). Glucoiberin (73) and glucoibervirin (95) were identified using GSLs isolated from Iberis umbellata [32 (link)]. All other chemicals and reagents were of analytical grade. Human cancer cell lines (bladder T24, bladder T24, and breast MDA-MB-231, acquired from the American Type Tissue Culture Collection (ATCC, Manassas, VA, USA)), were cultured in a humidified atmosphere with 5% CO₂ at 37 °C in Dulbecco’s modified Eagle medium (DMEM, Euro-Clone, Milano, Italy) containing 4.5 g/L glucose, 10% fetal bovine serum (FBS), and 1% antibiotics (Penicillin Streptomycin, EuroClone, Milano, Italy).
Additional purification steps are required for commercial sulfatase. Absolute ethanol was mixed with ultrapure water (30 mL) and 10 kU of aryl sulfatase (30 mL). The mixture was then centrifuged at 2650× g for 20 min at room temperature. The supernatant was dissolved in ethanol (90 mL). The mixture was further centrifuged at 1030× g for 15 min at room temperature, and the supernatants were removed and discarded. The combined pellets were thoroughly vortexed in ultrapure water (25 mL), transferred into 1 mL tubes, and frozen (−20 °C).

Publication 2023

4-hydroxyindol-3-ylmethylglucosinolate 4-methoxyglucobrassicin Antibiotics, Antitubercular Atmosphere Brassica Breast Bromides Cell Lines Clone Cells DEAE Sephadex Eagle Ethanol Fetal Bovine Serum Flowers Freezing Galactosialidosis glucobrassicin glucoerucin glucoiberin gluconasturtiin glucoraphanin Glucose glucotropeolin Helix (Snails) Homo sapiens Malignant Neoplasms neoglucobrassicin Pellets, Drug Penicillins Plant Roots Plants progoitrin sinigrin Stem, Plant Streptomycin Sulfatases Urinary Bladder

Top products related to «Sulfatases»

β glucuronidase by Merck Group

Sourced in United States, Germany, Switzerland

β-glucuronidase is an enzyme that catalyzes the hydrolysis of β-glucuronides. It is commonly used in laboratory settings for various analytical and research applications.

Sulfatase by Merck Group

Sourced in United States, Germany

Sulfatase is a lab equipment product offered by Merck Group. It is an enzyme that hydrolyzes sulfate esters, cleaving the sulfate group from a substrate molecule.

Formic acid by Merck Group

Sourced in Germany, United States, Italy, United Kingdom, France, Spain, China, Poland, India, Switzerland, Sao Tome and Principe, Belgium, Australia, Canada, Ireland, Macao, Hungary, Czechia, Netherlands, Portugal, Brazil, Singapore, Austria, Mexico, Chile, Sweden, Bulgaria, Denmark, Malaysia, Norway, New Zealand, Japan, Romania, Finland, Indonesia

Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.

Sodium acetate by Merck Group

Sourced in United States, Germany, United Kingdom, Spain, India, Italy, France, China, Poland, Canada, Australia, Ireland, Hungary, Mexico, Chile, Switzerland, Brazil, Macao, Netherlands, Belgium, New Zealand, Portugal, Czechia, Sweden, Sao Tome and Principe

Sodium acetate is a chemical compound with the formula CH3COONa. It is a common salt that is widely used in various laboratory and industrial applications. Sodium acetate functions as a buffer solution, helping to maintain a specific pH level in chemical reactions and processes.

Aryl sulfatase by Merck Group

Sourced in United States, Germany

Aryl sulfatase is a laboratory enzyme used in the analysis and characterization of biological samples. It functions by catalyzing the hydrolysis of aryl sulfate esters, which are commonly found in various biological matrices. This enzyme is utilized in research and diagnostic applications to assist in the study of sulfate metabolism and related biochemical processes.

Sulfatase from helix pomatia by Merck Group

Sourced in United States

Sulfatase from Helix pomatia is an enzyme preparation derived from the common garden snail. It exhibits sulfatase activity and can be used for the hydrolysis of sulfate esters in various applications.

Acetonitrile by Merck Group

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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.

Methanol by Thermo Fisher Scientific

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Methanol is a colorless, volatile, and flammable liquid chemical compound. It is commonly used as a solvent, fuel, and feedstock in various industrial processes.

Deae sephadex a 25 by Merck Group

Sourced in United States, Germany

DEAE-Sephadex A-25 is an anion exchange chromatography resin. It is composed of cross-linked dextran beads with diethylaminoethyl (DEAE) functional groups. The resin is designed for the separation and purification of biomolecules such as proteins, nucleic acids, and enzymes based on their ionic interactions.

Ammonium acetate by Merck Group

Sourced in United States, Germany, United Kingdom, Italy, Spain, India, France, China, Australia, Switzerland, Macao, Sao Tome and Principe, Canada, Ireland, Czechia, Belgium, Netherlands, Poland, Japan, Austria, Hungary, Finland, Mexico, Sweden, Romania

Ammonium acetate is a chemical compound with the formula CH3COONH4. It is a colorless, crystalline solid that is soluble in water and alcohol. Ammonium acetate is commonly used in various laboratory applications, such as pH adjustment, buffer preparation, and as a mobile phase component in chromatography.

What are Sulfatases and what is their biological significance?

Sulfatases are a class of enzymes that play a crucial role in the metabolism and regulation of sulfated biomolecules. They catalyze the hydrolysis of sulfate esters, enabling the degradation of glycosaminoglycans, desulfation of steroid hormones, and modulation of signaling pathways. These enzymes are found in a wide range of organisms, from bacteria to humans, and their dysregulation has been implicated in various diseases, such as lysosomal storage disorders and cancers. Understanding the structure, function, and regulation of sulfatases is an active area of research with implications for developing targeted therapies and improving our knowledge of sulfate-dependent biological systems.

What are the different types or variations of Sulfatases?

Sulfatases can be classified based on their substrate specificity and cellular localization. For example, there are arylsulfatases that hydrolyze aromatic sulfate esters, and glycosulfatases that target sulfated carbohydrates. Additionally, some sulfatases are found in the lysosome, while others are secreted or membrane-bound. The diversity of sulfatase types and their involvement in various metabolic processes highlights the complexity and importance of this enzyme family in biological systems.

What are some common applications of Sulfatases?

Sulfatases have a wide range of applications in both research and clinical settings. In research, they are used to study the metabolism and signaling pathways involving sulfated biomolecules, such as glycosaminoglycans and steroid hormones. Sulfatases are also employed in the characterization of sulfated oligosaccharides and the development of targeted therapies for diseases associated with sulfatase dysfunction, such as mucopolysaccharidoses and certain cancers. In the clinical context, sulfatase assays can be used for the diagnosis and monitoring of lysosomal storage disorders.

How can PubCompare.ai help optimize Sulfatase research?

PubCompare.ai's AI-driven protocol comparision can help researchers optimize their sulfatase studies in several ways. The platform allows you to screen protocol literature more efficiently, leveraging AI to pinpoint critical insights. By analyzing protocols from literature, preprints, and patents, PubCompare.ai can help you identify the most effective research methods related to sulfatases, ensuring improved reproducibility and accuracy. This streamlined solution enables researchers to choose the best protocols for their specific research goals, ultimately enhancing the quality and impact of their sulfatase-related studies.

What are some common challenges in working with Sulfatases?

One of the key challenges in working with sulfatases is the complexty of their substrate specificity and the diveristy of their biological functions. Researchers must carefully consider the type of sulfatase, its cellular localization, and the specific experimental conditions required to accurately measure its activity. Additionally, the regulation of sulfatase expression and activity can be influenced by various factors, making it important to understand the underlying mechanisms. Proper sample preparation and the selection of appropriate assay methodologies are also crucial for obtaining reliable and reproducible results when studying sulfatases.

More about "Sulfatases"

Sulfatases are a class of enzymes responsible for the hydrolysis of sulfate esters, playing a crucial role in the metabolism and regulation of sulfated biomolecules.
These versatile enzymes are involved in diverse biological processes, including the degradation of glycosaminoglycans, the desulfation of steroid hormones, and the modulation of signaling pathways.
Sulfatases can be found across a wide range of organisms, from bacteria to humans, and their dysregulation has been implicated in various diseases, such as lysosomal storage disorders and cancers.
Closely related to sulfatases are β-glucuronidases, which catalyze the hydrolysis of glucuronic acid conjugates.
Formic acid and sodium acetate are common buffers used in sulfatase research, while aryl sulfatases, such as the one derived from the Helix pomatia snail, are often utilized as model enzymes.
Acetonitrile and methanol are commonly used solvents in the purification and analysis of sulfatases, often in conjunction with ion-exchange chromatography techniques like DEAE-Sephadex A-25 and ammonium acetate.
Understanding the structure, function, and regulation of sulfatases is an active area of research, with important implications for developing targeted therapies and improving our knowledge of sulfate-dependent biological systems.
PubCompare.ai's AI-driven protocol comparision can help researchers optimize their sulfatase studies, ensuring improved reproducibility and accuracy through the identification of the most effective research methods from literature, preprints, and patents.