One 96-well plate (Costar) was coated with 100 μl (12.5 μg/ml) of the anti-DR monoclonal antibody L243 diluted in 12.5 mM borate buffer and incubated overnight at 4°C as previously described (15 (link)). In a second plate (Costar), 1 μl (50 μM) of each biotinylated peptide diluted in DMSO (Sigma-Aldrich) was placed in duplicate wells; 200 μl of purified MHC molecules (0.004 μg/ml) diluted in citrate phosphate buffer, pH 5.4, with 0.75% n-octyl-β-D-glucopyranoside (Sigma-Aldrich) and 1 mM PefaBloc (Roche) were then added to each well and incubated overnight at 37°C in a humidified chamber. The following day, the antibody plate was washed five times with 0.05% Tween-20 in PBS, pH 7.4, and blocked with 5% FCS in PBS for 3 h at room temperature. After washing, 50 μl of 50 mM Tris, pH 8.0, with 0.75% n-octyl-β-D-glucopyranoside was added to each well, and MHC–peptide complexes were transferred to the antibody plate and incubated overnight at 4°C. The following day, 0.1 mg/ml europium-labeled streptavidin diluted in assay buffer was added to each well and incubated for 30 min at room temperature followed by enhancement buffer (each from PerkinElmer) for 10–15 min. Fluorescence was then measured with a multilabel counter (Victor2 1420; PerkinElmer). The half max binding concentration of OspA163–175 was defined as the concentration of OspA peptide required for the binding of half of the MHC molecules compared with the positive control peptide.
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Pefabloc
Pefabloc
Pefabloc is a serine protease inhibitor used in biomedical research to prevent unwanted proteolytic digestion.
It is commonly utilized in experiments involving protein extraction, purification, and stabilization.
Pefabloc acts by irreversibly blocking the active sites of serine proteases, making it a valuable tool for preserving protein integrity and activity.
Researchers can leverage Pefabloc to enhance the reproducibility and reliability of their experimental protocols, particularly in areas such as enzyme kinetics, protein-protein interactions, and downstream applications like Western blotting and mass spectrometry.
By carefully selecting and optimizing Pefabloc-based procedures, scientists can obtain more consistent and meaningful results, contributing to the advancement of their pefabled* research.
It is commonly utilized in experiments involving protein extraction, purification, and stabilization.
Pefabloc acts by irreversibly blocking the active sites of serine proteases, making it a valuable tool for preserving protein integrity and activity.
Researchers can leverage Pefabloc to enhance the reproducibility and reliability of their experimental protocols, particularly in areas such as enzyme kinetics, protein-protein interactions, and downstream applications like Western blotting and mass spectrometry.
By carefully selecting and optimizing Pefabloc-based procedures, scientists can obtain more consistent and meaningful results, contributing to the advancement of their pefabled* research.
Most cited protocols related to «Pefabloc»
Antibodies, Anti-Idiotypic
Biological Assay
Borates
Buffers
Citrates
Europium
Fluorescence
Immunoglobulins
Pefabloc
Peptides
Phosphates
Streptavidin
Sulfoxide, Dimethyl
Tromethamine
Tween 20
For purification, 1 kg of cells was suspended in buffer A (250 mM Tris–HCl pH 8, 40% glycerol, 250 mM ammonium sulfate, 1 mM EDTA, 10 mM MgCl2, 10 µM ZnCl2, 12 mM β-mercaptoethanol) supplemented with protease-inhibitor cocktail (cOmplete EDTA-free, Roche) and lysed at 4°C with glass beads in a BeadBeater (BioSpec). The soluble fraction obtained after centrifugation (1 h at 14 000 rev min−1 in a Beckmann JA14 rotor) was loaded onto Heparin Sepharose (GE Healthcare) equilibrated in buffer A. The column was washed with buffer B (50 mM Tris–HCl pH 8, 250 mM ammonium sulfate, 0.5 mM EDTA, 1 mM MgCl2, 10 µM ZnCl2, 1 mM β-mercaptoethanol, 0.5 mM PMSF) and the complex was eluted from the resin with buffer B* (buffer B with 1 M ammonium sulfate). The sample was diluted to 500 mM ammonium sulfate and incubated with 10 ml pre-equilibrated IgG Sepharose (GE Healthcare) for 6 h. After washing with ten column volumes of buffer C (50 mM Tris–HCl pH 8, 20% glycerol, 225 mM ammonium sulfate, 0.5 mM EDTA, 1 mM MgCl2, 10 µM ZnCl2, 2 mM β-mercaptoethanol, 1 mg ml−1 Pefabloc), the IgG beads were mixed with Tobacco etch virus (TEV) protease and incubated overnight at 4°C in the same buffer. The supernatant was recovered and the resin was further washed with ten column volumes of buffer C* (buffer C without glycerol and with only 60 mM ammonium sulfate). The sample was subsequently purified by ion exchange on a Mono Q column (GE Healthcare); elution was performed using a gradient from 60 mM to 1 M ammonium sulfate in buffer D (40 mM Tris–HCl pH 8, 0.5 mM EDTA, 1 mM MgCl2, 10 µM ZnCl2, 1 mg ml−1 Pefabloc, 10 mM DTT). Pol I and Pol III eluted at ∼250 and ∼350 mM ammonium sulfate, respectively. The sample was concentrated to 6.5–7 mg ml−1 before crystallization.
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2-Mercaptoethanol
Buffers
Cells
Centrifugation
Crystallization
Edetic Acid
Glycerin
heparin-sepharose
immunoglobulin G-sepharose
Ion Exchange
Magnesium Chloride
Mono Q
Pefabloc
Protease Inhibitors
Resins, Plant
RNA Polymerase I
Sulfate, Ammonium
TEV protease
Tromethamine
Cultures of S. cerevisiae for protein purification were grown, harvested, and frozen as previously described (Reck-Peterson et al., 2006 (link)). Dynein constructs were purified via their ZZ tag, labeled with HaloTag-TMR or HaloTag-PEG-biotin ligands (Promega), and eluted into a modified TEV buffer (50 mM Tris-HCl [pH 8.0], 150 mM potassium acetate, 2 mM magnesium acetate, 1 mM EGTA, 10% glycerol, 1 mM DTT, 1 mM PMSF, and 0.1 mM Mg-ATP). Nudel was similarly purified via its ZZ tag, with the exception that the lysis buffer additionally contained a phosphatase inhibitor cocktail (Roche), and all buffers lacked Mg-ATP.
Lis1 constructs were purified via His8 and ZZ tags. Lysed cells were resuspended in Buffer A (final concentrations: 50 mM potassium phosphate [pH 8.0], 150 mM potassium acetate, 150 mM NaCl, 2 mM magnesium acetate, 5 mM β-mercaptoethanol, 10% glycerol, 0.2% Triton X-100, 0.5 mM Pefabloc, and 1 mM PMSF) supplemented with 10 mM imidazole (pH 7.5). Subsequent steps were at 4°C unless indicated. The lysate was clarified by centrifugation at 264,900 g for 1 hr. The supernatant was incubated with Ni-NTA agarose (QIAGEN) for 1 hr, transferred into a column, washed three times with Buffer A + 20 mM imidazole, and eluted with Buffer A + 250 mM imidazole. Eluted protein was then incubated with IgG sepharose beads (Amersham Pharmacia) for 1 hr, transferred into a column, and washed twice with Buffer A + 20 mM imidazole and once with TEV buffer (10 mM Tris-HCl [pH 8.0], 150 mM KCl, 10% glycerol, 0.2% Triton X-100, 1 mM PMSF, and 1 mM DTT). Lis1 was released from beads via incubation with TEV protease for 1 hr at 16°C, resulting in cleavage from the His8-ZZ tag.
Lis1 constructs were purified via His8 and ZZ tags. Lysed cells were resuspended in Buffer A (final concentrations: 50 mM potassium phosphate [pH 8.0], 150 mM potassium acetate, 150 mM NaCl, 2 mM magnesium acetate, 5 mM β-mercaptoethanol, 10% glycerol, 0.2% Triton X-100, 0.5 mM Pefabloc, and 1 mM PMSF) supplemented with 10 mM imidazole (pH 7.5). Subsequent steps were at 4°C unless indicated. The lysate was clarified by centrifugation at 264,900 g for 1 hr. The supernatant was incubated with Ni-NTA agarose (QIAGEN) for 1 hr, transferred into a column, washed three times with Buffer A + 20 mM imidazole, and eluted with Buffer A + 250 mM imidazole. Eluted protein was then incubated with IgG sepharose beads (Amersham Pharmacia) for 1 hr, transferred into a column, and washed twice with Buffer A + 20 mM imidazole and once with TEV buffer (10 mM Tris-HCl [pH 8.0], 150 mM KCl, 10% glycerol, 0.2% Triton X-100, 1 mM PMSF, and 1 mM DTT). Lis1 was released from beads via incubation with TEV protease for 1 hr at 16°C, resulting in cleavage from the His8-ZZ tag.
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2-Mercaptoethanol
Biotin
Buffers
Cells
Centrifugation
Classical Lissencephaly
Cytokinesis
Dynein ATPase
Egtazic Acid
Freezing
G 264
Glycerin
HaloTag
imidazole
immunoglobulin G-sepharose
Ligands
magnesium acetate
Pefabloc
Phosphoric Monoester Hydrolases
Potassium Acetate
potassium phosphate
Promega
Proteins
Sepharose
Sodium Chloride
TEV protease
Triton X-100
Tromethamine
For each independent purification, two forebrains were homogenized in DOC buffer (50 mM Tris pH 9.0, 1% sodium deoxycholate, 50 mM NaF, 20 μM ZnCl, 1 mM Na3VO4, 2 mM Pefabloc SC (Roche) and 1 tablet/10 ml protease inhibitor cocktail tablets (Roche)) and clarified as described earlier (Husi and Grant, 2001 (link)). A total of 25 mg of protein was incubated Dynal beads coupled with FLAG antibody for 2 h at 4°C. The resin was washed with three cycles of 15 resin volumes of DOC buffer and twice with TEV-protease cleavage buffer (Invitrogen). The tagged protein was cut from the beads by addition of TEV protease and the protein eluate was collected. The eluate was dialyzed against 2 L of dialysis buffer (50 mM sodium phosphate pH 8.0, 50 mM NaCl) at 4°C with constant agitation. After dialysis the supernatant was collected and added to Ni2+–NTA–agarose resin (Qiagen) pre-washed thrice with the dialysis buffer. The coupling was carried out for 40 min at 4°C with constant agitation in batch, then collected with supernatant and packed into 5 ml plastic columns (Clontech). After sedimentation, the supernatant was collected by gravity flow and the resin was washed thrice with wash buffer containing 0.1% sodium deoxycholate and 1 mM of imidazole. The elution was carried out with 750 μl of elution buffer and fractions were recovered.
All imidazole eluted fractions from the tandem purification that contained PSD-95 were pooled, concentrated in a Vivaspin concentrator (Vivascience, GE), reduced with DTT, alkylated with iodoacetamide and separated by one-dimensional SDS-electrophoresis 4–12% (NUPAGE, Invitrogen, CA). The gel was fixed and stained with colloidal Coomassie and entire gel lanes corresponding to the single-step and tandem purifications from PSD-95TAP/TAP, and wt forebrains were cut into slices and each slice was destained and digested overnight with trypsin (Roche, Trypsin modified, sequencing grade). A solution digest was carried out on the same quantity of starting material as the gel analyzed PSD-95TAP−TAP and wt purifications. Solution digests were carried out using sequencing grade, modified trypsin (Promega) for 4.5 h at 37°C.
All imidazole eluted fractions from the tandem purification that contained PSD-95 were pooled, concentrated in a Vivaspin concentrator (Vivascience, GE), reduced with DTT, alkylated with iodoacetamide and separated by one-dimensional SDS-electrophoresis 4–12% (NUPAGE, Invitrogen, CA). The gel was fixed and stained with colloidal Coomassie and entire gel lanes corresponding to the single-step and tandem purifications from PSD-95TAP/TAP, and wt forebrains were cut into slices and each slice was destained and digested overnight with trypsin (Roche, Trypsin modified, sequencing grade). A solution digest was carried out on the same quantity of starting material as the gel analyzed PSD-95TAP−TAP and wt purifications. Solution digests were carried out using sequencing grade, modified trypsin (Promega) for 4.5 h at 37°C.
Buffers
Cytokinesis
Deoxycholic Acid, Monosodium Salt
Dialysis
Electrophoresis
Gravity
imidazole
Immunoglobulins
Iodoacetamide
Pefabloc
Promega
Prosencephalon
Protease Inhibitors
Proteins
Resins, Plant
Sepharose
Sodium Chloride
sodium phosphate
Staphylococcal Protein A
TEV protease
Tromethamine
Trypsin
Plasmid transfection and RNAi were performed as described previously (Hanisch et al., 2006a (link)). Sgo1, aurora B, Hec1, TOGp, Ska1, Ska2, CENP-F, and Mad2 siRNA oligonucleotides were described previously (Honda et al., 2003 (link); Holt et al., 2005 (link); McGuinness et al., 2005 (link); Hanisch et al., 2006b (link)). Astrin, separase, and CENP-E were targeted with 5′-TCCCGACAACTCACAGAGAAA-3′, 5′-AAGCTTGTGATGCCATCCTGA-3′, and 5′-ACTCTTACTGCTCTCCAGTTT-3′ (QIAGEN), respectively. For Western blot analysis of whole cell lysate, cells of one 2-cm plate were harvested and lysed in laemmli buffer. For Western blot analysis of mitotic cells, HeLa S3 cells were collected by mitotic shake off and lysed in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 40 mM β-glycerolphosphate, 10 mM NaF, 0.3 mM Na-vanadate, 1 mM EDTA, 1% [vol/vol] IGEPAL, 0.1% [vol/vol] deoxycholate, 2 mM Pefabloc, 100 nM okadaic acid, and protease inhibitor cocktail without EDTA (Roche Diagnostics). For the analysis of separase activity by Western blotting, N-ethylmaleimide (2.5-mM final concentration; Sigma-Aldrich) was added to the lysis buffer.
astrin
AURKB protein, human
Buffers
Cells
Deoxycholate
Diagnosis
Edetic Acid
Ethylmaleimide
Glycerophosphates
HeLa Cells
Laemmli buffer
NDC80 protein, human
Okadaic Acid
Oligonucleotides
Pefabloc
Plasmids
Protease Inhibitors
RNA, Small Interfering
RNA Interference
Separase
SGOL1 protein, human
Sodium Chloride
Transfection
Tremor
Tromethamine
Vanadates
Western Blot
Most recents protocols related to «Pefabloc»
Inhibition of activity was assessed by testing the effect of EDTA and Pefabloc® on protease activity. For the EDTA assay, 2 μL protease was added to the reaction buffer with no added CaCl2 (protease solution contributed with 63 μM CaCl2 from the maturation step) and 0–1 mM EDTA and incubated for 60 min. For the Pefabloc® assay, 5 μL matured protease was added to the reaction buffer with calcium in 0–5 mM Pefabloc®. Tris at pH 7.5 was used in the reaction buffer to reduce the auto-hydrolysis of Pefabloc®. The protease was incubated with Pefabloc for 2.5 h RT.
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Biological Assay
Buffers
Calcium
Edetic Acid
Endopeptidases
Hydrolysis
Pefabloc
Psychological Inhibition
Tromethamine
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Aspergillus niger
Bath
Bile
Bos taurus
Capsaicin
Digestion
dihydrocapsaicin
Food
Intestines
Lipase
Mucosa, Gastric
Pancreas
Pancreatin
Pefabloc
Pepsin A
Pigs
Polysorbate 80
Proteins
Soybean oil
Stomach
Tween 80
Whey Proteins
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Centrifugation
Digestion
Emulsions
Enzymes
Exhaling
Filtration
Gastrointestinal Tract
High-Performance Liquid Chromatographies
Intestinal Absorption
Intestines
Micelles
Pefabloc
Vacuoles of GFP-Sch9 expressing WT, pho85Δ, and fab1Δ cells were isolated as described before [130 (link)], with the exception of some minor changes. Yeast cultures were grown in YPD to approximately OD600nm 1. Cells were harvested, washed once, and resuspended in 0,03 M Tris-HCl pH 8,9 containing 10 mM DTT. After a 10 min incubation at 30°C, cells were incubated at 30°C in spheroplasting buffer (YP 0.2% glucose; 0.6 M sorbitol; 50 mM KPi; 0.1 mM pefabloc; 6U zymolyase/OD600nm unit) for at least 30 min. The collected spheroplastes are resuspended in 15% ficoll buffer (15% ficoll; 10 mM PIPES/KOH pH 6.8; 0.2 M sorbitol; 0.1 mM pefabloc, 0.1 μg/ml leupeptin, 10 μg/ml o-phenantrolin, 0.5 μg/ml pepstatin A), to which 50 μl of 0.4 mg/ml diethylaminoethyl (DEAE) dextran was added per 100 OD600nm units of cells. After 2 min incubation on ice, followed by 2 min at 30°C, the spheroplast suspension was transferred to a transparent SW41 tube (Beckman Coulter, Suarlée, Belgium). 8% ficoll buffer, 4% ficoll buffer and 0% ficoll buffer were pipetted carefully on top to create a discontinuous ficoll gradient. The samples were centrifuged for 90 min at 30’000 rpm in a SW41 rotor, at 4°C (Beckman Coulter, Suarlée, Belgium). After collecting the vacuolar fraction from the 0% - 4% ficoll interphase, vacuolar vesicles were further concentrated by diluting ½ in 10 mM PIPES/KOH pH 6.8 and centrifugation for 10 min at 5200g, 4°C. The purity of the isolated vacuolar vesicles was monitored by Western analysis, using Anti-Vph1 (Abcam, Cambridge, UK), anti-ATP6V1A (Abcam, Cambridge, UK), anti-Porin (Invitrogen, Thermo Fisher Scientific, Merelbeke, Belgium), anti-Pma1 (kindly provided by B. André), anti-Dpm1 (Invitrogen, Thermo Fisher Scientific, Merelbeke, Belgium). Total protein concentrations were measured with the Bradford method (Bio-Rad, Temse, Belgium). The obtained vacuolar vesicles were diluted to 0.1 μg/μl in 10 mM PIPES/KOH pH 6.8 and stained with 8 μM FM4-64 (Invitrogen, Thermo Fisher Scientific, Merelbeke, Belgium). GFP and FM4-64 signal intensity was measured with the Fluoroskan Ascent FL Microplate Fluorometer (Thermo Fisher Scientific, Merelbeke, Belgium), using a 485/518 filter pair and 530/645 filter pair respectively. The GFP ratio’s relative to FM4-64 or protein content in each sample was determined to serve as a measure of GFP-Sch9 abundance at the vacuolar membrane.
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Buffers
Cells
Centrifugation
DEAE-Dextran
Ficoll
FM 4-64
Glucose
Interphase
leupeptin
Pefabloc
pepstatin
piperazine-N,N'-bis(2-ethanesulfonic acid)
Porin
Proteins
Sorbitol
Spheroplasts
Tissue, Membrane
Tromethamine
Vacuole
Yeast, Dried
zymolyase
HA2-Pho85, HA2-Pho85E53A (kinase-dead), and Pho80-GST were purified based on the description in [31 (link)]. The pho85Δ strain was transformed with plasmids pVW883, pVW884, and p946 (S2 Table ). Cells were grown overnight in SD -Ura liquid medium. In the morning cells were diluted at 0.2 OD600nm in 2 L SD -Ura. To induce Pho80-GST expression, cells were treated with 500 μM CuSO4 for 1 h, before harvesting the cells. Cells were collected by filtration, frozen in liquid nitrogen, and cryogenically disrupted by using a Precellys homogenizer in 10 ml of lysis buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 0.5 mM EDTA, 0.1% NP-40, 10% glycerol, 1 mM PMSF, 1 mM DTT, 400 mM Pefabloc, Roche complete protease inhibitor EDTA-free) in the presence of acid-washed glass beads. The cleared lysate was incubated for 2 h at 4°C with anti-HA magnetic beads (Fisher Scientific AG, Basel, Switzerland) for HA2-Pho85 and HA2-Pho85E53A purifications and glutathione magnetic agarose beads (Fisher Scientific AG, Basel, Switzerland) for Pho80-GST purification. After 5 washes with lysis buffer, HA-beads coupled with Pho85 or Pho85E53A were resuspended in 250 μL of elution buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) and stored at 80°C after addition of 10% glycerol. GST-coupled beads with Pho80 were eluted at room temperature in 250 μL of elution buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 mM L-glutathione reduced) for 2h.
Yeast cells bearing the plasmids for Sch9R650-I824-TAP expression were grown overnight in SRaffinose-Ura supplemented with 0.01% sucrose. The day after, at 0.2 OD600nm, 2% final galactose was added to the cells for 6 h, to induce Sch9R650-I824-TAP expression. Cells were collected by filtration, frozen in liquid nitrogen, and cryogenically disrupted by using Precellys homogenizer in 10 mL of lysis buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 0.5 mM EDTA, 0.1% NP-40, 10% glycerol, 400 mM Pefabloc, Roche complete protease inhibitor EDTA-free). The cleared lysate was incubated with IgG-coupled Dynabeads M-270 (Thermo Fisher Scientific, Basel, Switzerland) for 2h at 4°C. After 5 washes with lysis buffer, Sch9R650-I824 was eluted in 150 μL TEV buffer (50mM Tris-HCl pH 7.5, 0.5mM EDTA,) with 2% TEV protease and stored at 80°C after the addition of 10% glycerol. Purified proteins were separated by SDS-PAGE, and stained with Sypro Ruby (Invitrogen, Thermo Fisher Scientific, Basel, Switzerland) to perform a quantification.
Yeast cells bearing the plasmids for Sch9R650-I824-TAP expression were grown overnight in SRaffinose-Ura supplemented with 0.01% sucrose. The day after, at 0.2 OD600nm, 2% final galactose was added to the cells for 6 h, to induce Sch9R650-I824-TAP expression. Cells were collected by filtration, frozen in liquid nitrogen, and cryogenically disrupted by using Precellys homogenizer in 10 mL of lysis buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 0.5 mM EDTA, 0.1% NP-40, 10% glycerol, 400 mM Pefabloc, Roche complete protease inhibitor EDTA-free). The cleared lysate was incubated with IgG-coupled Dynabeads M-270 (Thermo Fisher Scientific, Basel, Switzerland) for 2h at 4°C. After 5 washes with lysis buffer, Sch9R650-I824 was eluted in 150 μL TEV buffer (50mM Tris-HCl pH 7.5, 0.5mM EDTA,) with 2% TEV protease and stored at 80°C after the addition of 10% glycerol. Purified proteins were separated by SDS-PAGE, and stained with Sypro Ruby (Invitrogen, Thermo Fisher Scientific, Basel, Switzerland) to perform a quantification.
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Acids
Buffers
Cells
Edetic Acid
Filtration
Freezing
Galactose
Glutathione
Glycerin
Nitrogen
Nonidet P-40
Pefabloc
Phosphotransferases
Plasmids
Protease Inhibitors
Proteins
SDS-PAGE
Sepharose
Sodium Chloride
Strains
Sucrose
Sypro Ruby
TEV protease
Tromethamine
Yeast, Dried
Top products related to «Pefabloc»
Sourced in Germany, United States, Canada, Switzerland, United Kingdom, France, Japan
Pefabloc is a serine protease inhibitor used for the prevention of protein degradation in samples. It effectively inhibits a wide range of serine proteases, including trypsin, chymotrypsin, and thrombin.
Sourced in United States, Germany, France, United Kingdom
Pefabloc is a protease inhibitor that is used in laboratory settings to prevent the degradation of proteins during sample preparation and analysis. It acts by inhibiting a broad range of serine proteases, including trypsin, plasmin, and thrombin. Pefabloc is a colorless, crystalline powder that is soluble in water and other aqueous solutions.
Sourced in United States, Germany, Italy
Pefabloc SC is a protease inhibitor that inactivates a broad range of serine proteases. It functions by irreversibly blocking the active site of proteases, preventing their enzymatic activity. Pefabloc SC is commonly used in research and industrial applications to inhibit unwanted proteolytic activity.
Sourced in Germany, United States, United Kingdom
Pefabloc SC is a serine protease inhibitor used in research and laboratory applications. It is a broad-spectrum inhibitor that effectively blocks the enzymatic activity of various serine proteases. Pefabloc SC is commonly used in sample preparation and protein purification procedures to prevent protease-mediated degradation of target proteins.
Sourced in United States, Germany, Switzerland, United Kingdom, China, France, Japan, Canada, Spain, Belgium, Australia, Sweden, Italy, Ireland, Macao
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.
Sourced in United States, Germany, China, United Kingdom, Italy, Japan, Sao Tome and Principe, France, Canada, Macao, Switzerland, Spain, Australia, Israel, Hungary, Ireland, Denmark, Brazil, Poland, India, Mexico, Senegal, Netherlands, Singapore
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.
Sourced in United States, Germany, Italy, China, Japan, France, Israel, Switzerland, Canada, Sao Tome and Principe, United Kingdom, Australia, Ireland
Leupeptin is a protease inhibitor that can be used in laboratory settings to inhibit the activity of certain proteases. It is a tripeptide compound that binds to and inhibits the catalytic sites of proteases.
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Aprotinin is a protease inhibitor derived from bovine lung tissue. It is used as a laboratory reagent to inhibit protease activity in various experimental procedures.
Sourced in United States, Switzerland, Germany, China, United Kingdom, France, Canada, Japan, Italy, Australia, Austria, Sweden, Spain, Cameroon, India, Macao, Belgium, Israel
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.
Sourced in United States, United Kingdom, Germany, Italy, Australia, Spain, China, Japan, France, Canada, Belgium, Czechia, Sweden
The DC protein assay kit is a colorimetric-based protein quantification method developed by Bio-Rad. It allows for the determination of protein concentration in aqueous solutions.
More about "Pefabloc"
Pefabloc, also known as 4-(2-Aminoethyl)benzenesulfonyl fluoride (AEBSF), is a powerful serine protease inhibitor that plays a crucial role in biomedical research.
This versatile compound is commonly utilized to prevent unwanted proteolytic digestion, ensuring the integrity and stability of proteins during various experimental procedures.
One of Pefabloc's primary applications is in the extraction, purification, and stabilization of proteins.
By irreversibly blocking the active sites of serine proteases, Pefabloc effectively preserves the native structure and function of proteins, making it an invaluable tool for researchers studying enzyme kinetics, protein-protein interactions, and downstream applications like Western blotting and mass spectrometry.
Pefabloc SC, a closely related compound, shares many of the same properties and uses as Pefabloc.
Both inhibitors can be employed in conjunction with other protease inhibitors, such as the Complete protease inhibitor cocktail or individual inhibitors like Leupeptin and Aprotinin, to create a comprehensive and robust system for protecting proteins from degradation.
Researchers can leverage Pefabloc-based procedures to enhance the reproducibility and reliability of their experimental protocols, leading to more consistent and meaningful results.
By carefully selecting and optimizing the use of Pefabloc, scientists can contribute to the advancement of their pefabled* research and unlock new insights in various fields of study.
In addition to its role in protein preservation, Pefabloc can also be used in the DC protein assay kit, a widely employed method for determining the concentration of proteins in samples.
This integration highlights the versatility of Pefabloc and its ability to seamlessly integrate into various research workflows.
By understanding the nuances of Pefabloc and related compounds, researchers can make informed decisions and select the most appropriate strategies to ensure the success of their experiments and the integrity of their data.
This versatile compound is commonly utilized to prevent unwanted proteolytic digestion, ensuring the integrity and stability of proteins during various experimental procedures.
One of Pefabloc's primary applications is in the extraction, purification, and stabilization of proteins.
By irreversibly blocking the active sites of serine proteases, Pefabloc effectively preserves the native structure and function of proteins, making it an invaluable tool for researchers studying enzyme kinetics, protein-protein interactions, and downstream applications like Western blotting and mass spectrometry.
Pefabloc SC, a closely related compound, shares many of the same properties and uses as Pefabloc.
Both inhibitors can be employed in conjunction with other protease inhibitors, such as the Complete protease inhibitor cocktail or individual inhibitors like Leupeptin and Aprotinin, to create a comprehensive and robust system for protecting proteins from degradation.
Researchers can leverage Pefabloc-based procedures to enhance the reproducibility and reliability of their experimental protocols, leading to more consistent and meaningful results.
By carefully selecting and optimizing the use of Pefabloc, scientists can contribute to the advancement of their pefabled* research and unlock new insights in various fields of study.
In addition to its role in protein preservation, Pefabloc can also be used in the DC protein assay kit, a widely employed method for determining the concentration of proteins in samples.
This integration highlights the versatility of Pefabloc and its ability to seamlessly integrate into various research workflows.
By understanding the nuances of Pefabloc and related compounds, researchers can make informed decisions and select the most appropriate strategies to ensure the success of their experiments and the integrity of their data.