Membrane scaffold protein (MSP) for 13 nm9 (link) and 50 nm28 (link) NDs, the maltose sensor29 (link), neuronal (rat syb2, syntaxin-1A and SNAP-25B) and yeast (Snc2p, Sso1p and Sec9c (residues 401-651)) SNAREs, were purified as described previously12 (link). T-SNARE complexes bearing truncated SNAP-25B (corresponding to residues 1-197 and residues 1-186) were also prepared and studied; the former truncation mimics cleavage by botulinum neurotoxin A30 (link). To prepare t-SNARE vesicles, lipids (10% PE, 15% PS and 75% PC) and the t-SNARE heterodimer were incubated with the respective cargoes and 2% OG on ice for 30 min. Detergent was removed by addition of Biobeads (Bio-Rad) (1/3 volume) followed by gentle shaking (4°C, overnight). The mixture was extruded through 0.2 μM filter and the t-SNARE vesicles were purified by passing through a PD10 column (5 ml) equilibrated in reconstitution buffer (25 mM HEPES, pH 7.5, 100 mM KCl, 1 mM DTT). Finally, purified t-SNARE vesicles were dialyzed against reconstitution buffer (4°C, overnight). Reconstitution of syb2 into 13 nm NDs was performed as described9 (link). For reconstitution of syb2 into 50 nm NDs, the MSP/lipid ratio was 2:4000. To incorporate different copy numbers of syb2 into 50 nm NDs, the following MSP/syb2 ratios were used: 2:2 (ND3), 2:4 (ND5) and 2:10 (ND7). The reconstituted NDs were incubated with Ni2+-NTA resin to remove syb2-free NDs. NDs containing syb2 were eluted by reconstitution buffer with 0.4M imidazole. The NDs were further purified via sucrose density gradient centrifugation31 (link), followed by dialysis against reconstitution buffer (4°C, overnight). The copy number of syb2 per ND refers to the total number of syb2 molecules, not the number of copies per face of the ND.
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Biobeads
Biobeads
Biobeads are a versatile class of biomaterials used in a variety of research applications, including protein purification, drug delivery, and biosensing.
These bead-like structures are typically composed of synthetic or natural polymers and can be engineered to possess specific physical and chemical properties.
Researchers utilize Biobeads to optimize experimental protocols, enhance reproducibility, and uncover novel insights in their Biobeads-related studies.
PubCompare.ai offers an AI-powered platform to help scientists easily locate the most accurate and reproducible Biobeads research from literature, preprints, and patents, leveraging data-driven analysis to identify the best protocols and prodcuts for their work.
Experience seamless, data-driven decision making and optimize your Biobeads research with PubCompare.ai.
These bead-like structures are typically composed of synthetic or natural polymers and can be engineered to possess specific physical and chemical properties.
Researchers utilize Biobeads to optimize experimental protocols, enhance reproducibility, and uncover novel insights in their Biobeads-related studies.
PubCompare.ai offers an AI-powered platform to help scientists easily locate the most accurate and reproducible Biobeads research from literature, preprints, and patents, leveraging data-driven analysis to identify the best protocols and prodcuts for their work.
Experience seamless, data-driven decision making and optimize your Biobeads research with PubCompare.ai.
Most cited protocols related to «Biobeads»
Biobeads
Botulinum Toxins
Buffers
Cytokinesis
Detergents
Dialysis
Face
HEPES
imidazole
Lipids
Maltose
Membrane Lipids
Membrane Proteins
Neurons
Proteins
Resins, Plant
Saccharomyces cerevisiae
SNAP Receptor
Sucrose
Syntaxin-1A
Target Membrane SNARE Proteins
Allantois
alpha-Fetoproteins
Antibodies, Anti-Idiotypic
Antigens
Biobeads
Biological Assay
Calcium chloride
Centrifugation
Child
Enzyme Stability
Immunoglobulins
Influenza A Virus, H3N2 Subtype
Lectin
Peanut Agglutinin
Peroxidase
Phosphoric Acids
Serum
Technique, Dilution
Triton X-100
Vaccines
Virion
Virus
The 8B6 monoclonal antibody (mAb) against SERT was raised by Dan Cawley (Vaccine and Gene Therapy Institute; OHSU). StrepII tagged SERT was purified by Strep Tactin affinity as described subsequently in DDM with 1 μM paroxetine. Liposomes containing asolectin:cholesterol:lipid A:brain polar lipid (60:17:3:20) were prepared in TBS (20 mM Tris pH 8, 100 mM NaCl) at a concentration of 40 mg/ml−1 by extrusion through 200 nm filters. Liposomes were saturated with 5 mM n-dodecyl-β-D-maltoside (DDM) and purified SERT was added to the detergent:lipid mixture. DDM was removed by three successive additions of 80 mg/ml biobeads. For the first two additions, the biobeads were incubated for 2 hrs; the final incubation was overnight. 10 μM paroxetine was added to the proteoliposomes after reconstitution. SERT knockout mice were purchased from the Jackson Laboratory (mouse stain: 008355) and immunized with ~30 μg of reconstituted SERT. Hybridoma cell lines were generated as described51 (link) and screened by fluorescence-detection size-exclusion chromatography (FSEC)24 (link) and western blotting to select antibodies which recognize tertiary epitopes. The 8B6 mAb was purified from hybridoma supernatants using 4-mercapto-ethyl-pyridine resin. Fab was purified from papain digested mAb by cation exchange chromatography and was stored in 20 mM Tris pH 8, 150 mM NaCl, 10% glycerol.
The sequences of the 8B6 Fab light and heavy chain genes were determined by standard techniques. The genes of the 8B6 Fab were cloned into a bicistronic insect cell expression vector, including a GP67 signal peptide. A thrombin cleavage site and 8His tag were fused to the C-terminus of residues 1–235 of the heavy chain. The 8B6 Fab was purified from SF9 supernatant by metal ion affinity chromatography followed by cation exchange chromatography.
The sequences of the 8B6 Fab light and heavy chain genes were determined by standard techniques. The genes of the 8B6 Fab were cloned into a bicistronic insect cell expression vector, including a GP67 signal peptide. A thrombin cleavage site and 8His tag were fused to the C-terminus of residues 1–235 of the heavy chain. The 8B6 Fab was purified from SF9 supernatant by metal ion affinity chromatography followed by cation exchange chromatography.
4-mercaptoethylpyridine
Antibodies
asolectin
Biobeads
Brain
CD33 protein, human
Cell Lines
Cells
Cholesterol
Chromatography
Chromatography, Affinity
Cytokinesis
Detergents
Epitopes
Fluorescence
Gel Chromatography
Genes
Glycerin
Hybridomas
Insect Vectors
Light
Lipid A
Lipids
Liposomes
Metals
Mice, Knockout
Monoclonal Antibodies
Mus
Papain
Paroxetine
proteoliposomes
Resins, Plant
Signal Peptides
Sodium Chloride
Stains
Streptococcal Infections
Therapy, Gene
Thrombin
Tromethamine
Vaccines
Reconstituted proteoliposomes were prepared as described (Zick and Wickner, 2013 (link)), with modifications. Chloroform solutions of lipids (vacuolar mixed lipids; VML) were mixed in a glass vial: 49.6 or 51 mol % diC18:2 PC, 15% diC18:2 PE, 1% diacylglycerol, 8% ergosterol, 2% diC18:2 PA, 18% soy PI, 4.4% diC18:2 PS, 1% diC16 PI(3)P and either 0.23% Marina Blue-PE or 1.5% NBD-PE (Life Technologies). When small headgroup lipids were omitted, the amount of PC was adjusted to bring the sum to 100%. β-octylglucoside was added to 160 mM from a 0.5 M solution in methanol and samples were dried under a stream of nitrogen, then in vacuo. Samples were dissolved in a fivefold concentrate of RB150+Mg (0.1 M HEPES/NaOH, pH 7.4, 0.75 M NaCl, 50% glycerol, 5 mM MgCl2) by several cycles of vortexing for 10 s, rocker mixing for 30 min, and bath sonication for 5 min, yielding mixed micellar solutions with 4 mM lipids and 50 mM detergent. Lipid micellar solutions (200 µl) were mixed with a mixed micellar solution of purified Ypt7p and the indicated SNAREs (550 µl) and 250 µl of either Cy5-derivatized streptavidin (from KPL, Gaithersburg, MD; 8 µM final) or biotinylated phycoerythrin (Life Technologies; 4 µM final). Each ml of solution was added to a rinsed and knotted 6 cm segment of SpectraPor dialysis membrane, 25 kDa cutoff, 7.5 mm diameter (Spectrum Labs, Rancho Dominguez, CA) which was then knotted and dialyzed at 4°C in 250 ml of RB150+Mg (20 mM HEPES, pH 7.4, 150 mM NaCl, 10% glycerol, 1 mM MgCl2 [Mima et al., 2008 (link); Zucchi and Zick, 2011 (link)]) with 1 g of BioBeads SM-2 (Biorad, Hercules, CA) for at least 20 hr with continuous stirring. The isolation of proteoliposomes by flotation was as described (Zick and Wickner, 2013 (link)). After total phosphate was assayed, samples were brought to 2 mM lipid with RB150+Mg and small aliquots were frozen in liquid nitrogen and stored at −80°C.
Bath
Biobeads
Chloroform
Detergents
Diacylglycerol
Dialysis
Ergosterol
Freezing
Glycerin
HEPES
isolation
Lipids
Magnesium Chloride
Methanol
Micelles
Mima
N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)phosphatidylethanolamine
Nitrogen
octyl glucoside
Phosphates
Phycoerythrin
proteoliposomes
RB150
SNAP Receptor
Sodium Chloride
Streptavidin
Tissue, Membrane
Vacuole
Integrin nanodiscs were assembled based on a protocol adapted from previous papers (Denisov et al., 2004 (link); Nath et al., 2007 (link)). In brief, DMPC and DMPG were solubilized in chloroform or a chloroform/methanol mixture, mixed thoroughly, and dried onto a glass tube under steady flow of nitrogen. The homogeneous lipid mixture was then solubilized in 100 mM cholate in 10 mM Tris and 100 mM NaCl, pH 7.4, giving a lipid concentration of 50 mM. 72 µl of the lipid solution was then mixed with 200 µl of 200 µM membrane scaffold protein (MSP) in dH2O and 200 µl of 10 µM purified inactive integrin (described earlier). The final ratio of lipids/MSP/protein is 90:1:0.05 in a total volume of 472 µl. The integrin nanodiscs were assembled by removing the detergents with SM-2 Biobeads overnight at room temperature. The assembled integrin nanodiscs were then purified with a hi-load 16/60 Superdex 200 size exclusion column with 20 mM Tris, 150 mM NaCl, and 0.5 mM CaCl2, pH 7.4, as the column buffer. The integrin nanodiscs and empty nanodiscs were readily separated (Fig. S2) and the successful assembly was verified by SDS-PAGE analysis. Two MSP constructs, MSP1D1 and MSP1E3D1 (Denisov et al., 2004 (link)) expressed and purified from bacteria, were used to make integrin nanodiscs and similar patterns of integrin activation results were obtained with both constructs.
Bacteria
Biobeads
Buffers
Chloroform
Cholate
Detergents
Dimyristoylphosphatidylcholine
dimyristoylphosphatidylglycerol
Integrins
Lipid A
Lipids
Membrane Lipids
Membrane Proteins
Methanol
Nitrogen
Proteins
SDS-PAGE
Sodium Chloride
Tromethamine
Most recents protocols related to «Biobeads»
To prepare TREK1 proteoliposomes in varied lipid compositions, chloroform solubilized 18:1–18:1 phosphatidylcholine (DOPC), POPA, or POPE lipids were combined in borosilicate glass vials to a final lipid concentration of 5 mg total lipid per reconstitution. Lipids were dried under nitrogen, washed once with pentane to remove residual chloroform, and redried into a thin lipid film under nitrogen, followed by overnight incubation under vacuum in a vacuum desiccator to fully dry the lipid mixtures. Lipids were then solubilized in HighK buffer (150 mM KCl, 20 mM HEPES, pH 7.4) supplemented with 8 mM CHAPS and sonicated until the solution was visually clear. The solubilized lipids were mixed with purified TREK1 protein (0.5 μg/mg lipid, unless otherwise indicated) and allowed to incubate at room temperature for 20 min, followed by the addition of 200 mg SM-2 biobeads (Bio-Rad) to remove the detergent and form proteoliposomes. Samples were rotated in the presence of biobeads for 2 h at room temperature and the formed proteoliposomes were then extruded through a 0.1 µm filter (Whatman) using a mini-extruder (Avanti Polar lipids), to produce uniform ~100 nm liposomes ready for ACMA studies. Proteoliposomes were made fresh for each experiment and used within 24 h of preparation.
For 9-Amino-6-Chloro-2-Methoxyacridine (ACMA) fluorescence quenching assays, our protocols mirror those of prior studies utilizing this assay for the study of K2P function21 ,35 ,61 . About 50 μl of freshly prepared TREK1 proteoliposomes were mixed with 2 ml of HighNa buffer (150 mM NaCl, 20 mM HEPES, pH 7.4) containing 2 μM ACMA and transferred to quartz cuvettes (Hellma) in a PTI quantamaster fluorimeter. Sixty seconds of baseline recording was captured (measurements taken every 0.2 s), with excitation at 410 ± 9 nm and emission measured at 490 ± 15 nm. ACMA quenching was initiated by the addition of the proton ionophore carbonyl cyanide 3-chlorophenylhydrazone (CCCP) to a final concentration of 1 μM. After quenching reactions plateaued, the potassium ionophore valinomycin was added to the reactions (final concentration 18 nM) to collapse the potassium gradient across the proteoliposome membrane and complete ACMA quenching. All traces were normalized to their individual baseline and post-valinomycin treated values (Fstart – F)/(Fstart - Fvalin), with Fstart defined as the final value of the first 60 s of recording prior to the addition of CCCP and Fvalin as the final time point in the recording once valinomycin treatment was completed.
For 9-Amino-6-Chloro-2-Methoxyacridine (ACMA) fluorescence quenching assays, our protocols mirror those of prior studies utilizing this assay for the study of K2P function21 ,35 ,61 . About 50 μl of freshly prepared TREK1 proteoliposomes were mixed with 2 ml of HighNa buffer (150 mM NaCl, 20 mM HEPES, pH 7.4) containing 2 μM ACMA and transferred to quartz cuvettes (Hellma) in a PTI quantamaster fluorimeter. Sixty seconds of baseline recording was captured (measurements taken every 0.2 s), with excitation at 410 ± 9 nm and emission measured at 490 ± 15 nm. ACMA quenching was initiated by the addition of the proton ionophore carbonyl cyanide 3-chlorophenylhydrazone (CCCP) to a final concentration of 1 μM. After quenching reactions plateaued, the potassium ionophore valinomycin was added to the reactions (final concentration 18 nM) to collapse the potassium gradient across the proteoliposome membrane and complete ACMA quenching. All traces were normalized to their individual baseline and post-valinomycin treated values (Fstart – F)/(Fstart - Fvalin), with Fstart defined as the final value of the first 60 s of recording prior to the addition of CCCP and Fvalin as the final time point in the recording once valinomycin treatment was completed.
1,2-oleoylphosphatidylcholine
1-palmitoyl-2-oleoylphosphatidylethanolamine
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate
9-amino-6-chloro-2-methoxyacridine
Biobeads
Biological Assay
Buffers
carbonyl 3-chlorophenylhydrazone
Carbonyl Cyanide m-Chlorophenyl Hydrazone
Chloroform
Detergents
Fluorescence
HEPES
Ionophores
Lipid A
Lipids
Liposomes
Neoplasm Metastasis
Nitrogen
pentane
Phosphatidylcholines
Potassium
potassium channel protein TREK-1
Potassium Ionophores
Preparation H
proteoliposomes
Protons
Quartz
Shock
Sodium Chloride
Tissue, Membrane
Vacuum
Valinomycin
Proteoliposomes were reconstituted by the method described (27 (link)) with slight modification. First, crude soybean L-α-phosphatidylcholine (type II-S; Sigma) was washed with acetone to remove K+ from the lipid. Next, the washed lipid was suspended in a reconstitution buffer (15 mM MES–tricine, 2 mM KOH, 5 mM NaCl, 2.5 mM MgCl2, and 50 mM sucrose, with pH adjusted to 8.0 with NaOH). The aliquots were then sonicated to disperse lipids and centrifuged at 125,000 × g at 20 °C for 30 min. The sonication and centrifugation were repeated three times. Then, the resulting lipid was suspended at a final concentration of 32 mg/mL in the reconstitution buffer. Finally, the suspended lipid was flash-frozen in liquid nitrogen and stored at −80 °C until use. The preparation of CFoCF1 proteoliposomes was performed as follows. First, the suspended lipid was mixed with an equal volume of 4% n-octyl-β-D-glucoside in the reconstitution buffer. Next, 100 mg of Biobeads (SM-2; Bio-Rad) was added in plural times to 1 mL of the solution and gently stirred until the solution became cloudy. CFoCF1 was then added to the solution gently to be the final concentration of 0.15 mg/mL. Biobeads were then added to the mixture to remove excess detergent, and the mixture was incubated at 4°C overnight, followed by flash-frozen in liquid nitrogen, and stored at −80°C until use (27 (link)).
To measure ATP synthesis activity, the acid–base transition method was used with the valinomycin-induced diffusion potential of K+ as described (34 (link)) with slight modification. The CFoCF1/lipid ratio of proteoliposomes was set to 90 μg/9.6 mg to accurately measure ATP synthesis activity in both redox states. Before acidification, the proteoliposomes were reduced with 50 mM DTT for 2 h at 30°C in the reconstitution buffer. No oxidizing treatment was done because the purified CFoCF1 was in a completely oxidized form (SI Appendix, Figs. S9B and S10 ). Following the reaction, proteoliposomes were incubated in the acid buffer for 20 min for acidification. ATP calibration was performed by adding 5 µL of 20 µM or 10 μM ATP three times. The details of the conditions for measuring ATP synthesis activity are shown in SI Appendix, Figs. S11 and S12 .
To measure ATP synthesis activity, the acid–base transition method was used with the valinomycin-induced diffusion potential of K+ as described (34 (link)) with slight modification. The CFoCF1/lipid ratio of proteoliposomes was set to 90 μg/9.6 mg to accurately measure ATP synthesis activity in both redox states. Before acidification, the proteoliposomes were reduced with 50 mM DTT for 2 h at 30°C in the reconstitution buffer. No oxidizing treatment was done because the purified CFoCF1 was in a completely oxidized form (
Acetone
Acids
Anabolism
Biobeads
Buffers
Centrifugation
Detergents
Diffusion
Figs
Freezing
Glucosides
Lipids
Magnesium Chloride
Nitrogen
Oxidation-Reduction
Phosphatidylcholines
proteoliposomes
Sodium Chloride
Soybeans
Sucrose
tricine
Valinomycin
Purified AdiC was mixed with POPC and the MSP2N2 membrane scaffold protein purified as described (Ritchie et al., 2009 (link); Denisov et al., 2019 (link)) in an 1:1500:10 molar ratio of the AdiC dimer:POPC:MSP2N2. The mixture was incubated at 4°C for at least 2 hr. Nanodiscs were assembled during a dialysis of the mixture against a buffer containing 100 mM NaCl, 20 mM Tris titrated to pH 8.0, and 0.5 mM TCEP at 4°C overnight. After the dialysis, the nanodiscs were labeled with biotin using the BirA Enzyme (Avidity) following the protocol provided by the manufacturer, and then mixed with bifunctional rhodamine in a 2:1 molar ratio of the AdiC dimer:bifunctional rhodamine, a ratio to maximize the chance of only one AdiC monomer in each dimer to be labeled; this mixture was incubated at room temperature for more than 4 hr. The remaining free dye was removed first with Biobeads (SM-2, Bio-Rad) and then by size-exclusion chromatography (Superose 6 10/30 or Superderx 200 10/300, GE) equilibrated with a solution containing 100 mM NaCl and 50 mM Tris titrated to pH 8.0. As expected, the peak of the protein containing the two mutant cysteine residues, detected at 280 nm, co-migrated with that of the fluorophore dye detected at 550 nm. In contrast, no notable absorbance peak at 550 nm co-migrated with the peak of the protein without these mutant cysteine residues. Thus, there was no detectable background labeling (Figure 1—figure supplement 1A and B ). The final product of nanodiscs harboring labeled AdiC was aliquoted, flash frozen in liquid nitrogen, and stored in a –80°C freezer.
Biobeads
Biotin
Buffers
Cysteine
Dialysis
Dietary Supplements
Enzymes
Freezing
Gel Chromatography
Membrane Proteins
Molar
Nitrogen
Proteins
Rhodamine
Sodium Chloride
tris(2-carboxyethyl)phosphine
Tromethamine
Membrane scaffold protein (MSP) 1D1 was expressed and purified following an established protocol (Martens et al., 2016 (link)). For lipid preparation, 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC, Avanti Polar Lipids), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE, Avanti Polar Lipids) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (POPG, Avanti Polar Lipids) were mixed at a molar ratio of 3:1:1, dried under Argon and resuspended with 14 mM DDM (Autzen et al., 2018 (link)). For nanodisc reconstitution, HsFpn, MSP1D1 and lipid mixture were mixed at a molar ratio of 1:2.5:50 and incubated on ice for 1 hr. Detergents were removed by the sequential addition of 60 mg/mL Biobeads SM2 (Bio-Rad) for three times over a 3-hr period. The sample was then incubated with Biobeads overnight at 4 °C. After removal of Biobeads, 11F9 was added to the sample at a molar ratio of 1.1:1 to HsFpn. The complex was incubated on ice for 30 min before being loaded onto a SEC column equilibrated with the FPLC buffer without detergent. The purified nanodisc sample was concentrated to 10 mg/ml and incubated with 2 mM CaCl2 for 30 min on ice before cryo-EM grid preparation.
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine
1-palmitoyl-2-oleoylphosphatidylethanolamine
Argon
Biobeads
Buffers
Detergents
Glycerin
Lipids
Martes
Membrane Proteins
Molar
Phosphorylcholine
An established protocol [25 (link)] was used to express and purify membrane scaffold protein (MSP) 1D1. Lipid preparation was carried out by mixing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC, Avanti Polar Lipids), POPE, and POPG at a molar ratio of 3:1:1. The lipid mixture was dried with Argon and vacuumed for 2 h. The lipid was resuspended with 14 mM DDM [26 (link)]. HsFpn, MSP1D1, and the lipid mixture were mixed at a molar ratio of 1:2.5:50 and incubated on ice for 1 h for nanodisc reconstitution. A total of 60 mg/mL of Biobeads SM2 (Bio-Rad) were added 3 times within 3 h to remove detergents. After the samples were incubated with the Biobeads overnight at 4°C, the Biobeads were removed. 11F9 Fab was added to the nanodisc sample at a molar ratio of 1.1:1 to Fpn. The complex was incubated on ice for 30 min before it was loaded onto a SEC column that had been equilibrated with 20 mM HEPES (pH 7.5) and 150 mM NaCl. The purified nanodisc sample was concentrated to 10 mg/ml and incubated with 10 mM CoCl2 or 1 mM PR73 for 30 min before cryo-EM grid preparation.
1-palmitoyl-2-oleoylphosphatidylethanolamine
Argon
Biobeads
Detergents
Glycerylphosphorylcholine
HEPES
Lipids
Membrane Proteins
Molar
Sodium Chloride
Top products related to «Biobeads»
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Bio-Beads SM-2 are macroporous polystyrene beads designed for size exclusion chromatography. They have a porous structure that allows for the separation of molecules based on their size and shape. The beads have a specified surface area and pore size distribution.
Sourced in United States, United Kingdom, Germany
Bio-Beads are a type of chromatographic media used for protein purification and separation. They are made of a cross-linked polymer matrix and are available in a range of bead sizes and properties to suit various applications. Bio-Beads provide a high surface area for effective adsorption and desorption of target molecules.
Sourced in United States, United Kingdom, Germany
SM2 Bio-Beads are porous polymeric beads designed for a variety of chromatographic applications. They feature a high surface area and controlled pore size, making them suitable for size-exclusion, adsorption, and other separation techniques.
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The Superdex 200 column is a size-exclusion chromatography media used for the separation and purification of proteins, peptides, and other biomolecules. It is designed to provide efficient separation and high resolution across a wide range of molecular weights. The column is suitable for a variety of applications, including protein analysis, desalting, and buffer exchange.
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The Mini-extruder is a compact and versatile laboratory device designed for the extrusion of lipid vesicles and liposomes. It features a manual operation mechanism that allows for controlled and reproducible extrusion of samples through polycarbonate membranes with defined pore sizes.
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Amphipol A8-35 is a non-ionic amphipathic polymer designed for the solubilization and stabilization of membrane proteins. It is composed of a polyacrylate backbone with alkyl side chains, providing both hydrophobic and hydrophilic properties. Amphipol A8-35 can be used to extract and maintain the native structure and function of membrane proteins in aqueous solutions.
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ATP is a laboratory instrument used to measure the presence and concentration of adenosine triphosphate (ATP) in various samples. ATP is a key molecule involved in energy transfer within living cells. The ATP product provides a reliable and accurate method for quantifying ATP levels, which is useful in applications such as microbial detection, cell viability assessment, and ATP-based assays.
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
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BioBeads SM-2 Adsorbent is a neutral, hydrophobic, polystyrene-based porous resin designed for the adsorption of small hydrophobic molecules. It has a surface area of approximately 800 m²/g and a pore size distribution centered around 30 Angstroms.
BioBeads are a versatile and advanced protein purification system developed by GE Healthcare. The core function of BioBeads is to efficiently capture and separate target proteins from complex mixtures, enabling effective purification for a wide range of applications.
More about "Biobeads"
Biobeads are a versatile class of biomaterials widely used in various research applications, including protein purification, drug delivery, and biosensing.
These bead-like structures are typically composed of synthetic or natural polymers and can be engineered to possess specific physical and chemical properties.
Researchers utilize Biobeads, such as Bio-Beads SM-2, Superdex 200 column, Mini-extruder, and Amphipol A8-35, to optimize experimental protocols, enhance reproducibility, and uncover novel insights in their studies.
Biobeads are also known as Bio-Beads or SM2 Bio-Beads, and they have been used in conjunction with other materials like ATP and Triton X-100 to enhance research outcomes.
The BioBeads SM-2 Adsorbent is a commonly used variant that helps in the purification and isolation of various biomolecules.
By leveraging the versatility and customizability of Biobeads, researchers can tailor their experimental setups to suit their specific needs, leading to more accurate and reproducible results.
PubCompare.ai, an AI-powered platform, can help scientists easily locate the most relevant and reliable Biobeads research from literature, preprints, and patents, enabling data-driven decision making and optimizing their Biobeads-related studies.
These bead-like structures are typically composed of synthetic or natural polymers and can be engineered to possess specific physical and chemical properties.
Researchers utilize Biobeads, such as Bio-Beads SM-2, Superdex 200 column, Mini-extruder, and Amphipol A8-35, to optimize experimental protocols, enhance reproducibility, and uncover novel insights in their studies.
Biobeads are also known as Bio-Beads or SM2 Bio-Beads, and they have been used in conjunction with other materials like ATP and Triton X-100 to enhance research outcomes.
The BioBeads SM-2 Adsorbent is a commonly used variant that helps in the purification and isolation of various biomolecules.
By leveraging the versatility and customizability of Biobeads, researchers can tailor their experimental setups to suit their specific needs, leading to more accurate and reproducible results.
PubCompare.ai, an AI-powered platform, can help scientists easily locate the most relevant and reliable Biobeads research from literature, preprints, and patents, enabling data-driven decision making and optimizing their Biobeads-related studies.