[125I]-AngII was prepared with the iodogen method, and specific activity was determined from self-displacement and saturation experiments, as previously described4 . The density of cell surface receptors was evaluated with binding assays at 4 °C using [125I]-AngII as the tracer. HEK293 cells expressing either AT1R or AT1R-RlucII were seeded 1 day after transfection at a density of ∼120,000 cells per well in poly-L -ornithine-coated 24-well plates. The following day, cells were washed once with pre-warmed DMEM with 20 mM HEPES (DMEM-H) and then incubated in the absence or presence of 100 nM AngII in DMEM-H for 30 min at 37 °C. The plates were quickly washed three times with ice-cold acid (50 mM sodium citrate, pH 4.0) for 5 min each on ice to stop the stimulation and remove both the remaining surface bound and unbound AngII ligand. To remove and neutralize the residual acid, cells were further washed twice with ice-cold Tyrode's buffer. Cells were incubated with 0.5 ml of [125I]-AngII (∼250,000 c.p.m. at ∼2000, ci mmol−1) in binding buffer (0.2% BSA, 50 mM Tris, 100 mM NaCl2, 5 mM MgCl2, pH 7.4) at 4 °C overnight. Non-specific binding was determined in the presence of 1 μM AngII. The next day, cells were washed three times with ice-cold PBS with calcium and magnesium, and 0.5 ml of 0.5 M NaOH/0.05% SDS was added. Radioactivity from solubilized cells was counted using a PerkinElmer Wizard 1470 automatic γ-counter.
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Iodo-Gen
Iodo-Gen
Iodo-Gen is a reagent used for the iodination of proteins and other macromolecules.
It is a mild, water-soluble oxidizing agent that can be used to label a variety of compounds with radioactive iodine, such as tyrosine and histidine residues in proteins.
Iodo-Gen is typically employed in immunoassays, receptor binding studies, and other applications where radiolabeled compounds are required.
The Iodo-Gen method offers improved labeling efficiency and milder oxidation conditions compared to alternative iodination techniques, making it a popular choice for preserving the biological activity of the labeled molecule.
It is a mild, water-soluble oxidizing agent that can be used to label a variety of compounds with radioactive iodine, such as tyrosine and histidine residues in proteins.
Iodo-Gen is typically employed in immunoassays, receptor binding studies, and other applications where radiolabeled compounds are required.
The Iodo-Gen method offers improved labeling efficiency and milder oxidation conditions compared to alternative iodination techniques, making it a popular choice for preserving the biological activity of the labeled molecule.
Most cited protocols related to «Iodo-Gen»
Acids
Biological Assay
Buffers
Calcium
Cells
Cold Temperature
HEK293 Cells
HEPES
Iodo-Gen
Ligands
Magnesium
Magnesium Chloride
polyornithine
Radioactivity
Sodium Citrate
Transfection
Tromethamine
The reference glycosphingolipids were isolated and characterized by mass spectrometry and proton NMR as described (15 (link)). Thin layer chromatography was done on aluminum- or glass-backed silica gel 60 high performance thin layer chromatography plates (Merck). Glycosphingolipid mixtures (40 μg)or pure compounds (2–8 μg) were eluted using chloroform/methanol/water (60:35:8, v/v/v) as a solvent system. Glycosphingolipids were detected by the anisaldehyde reagent (15 (link)) or the resorcinol reagent (16 (link)).
The mouse monoclonal antibodies tested for binding to the acid glycosphingolipids of hESC in the chromatogram binding assay are given insupplemental Table S2 . Binding of antibodies to glycosphingolipids separated on thin layer chromatograms was performed as described by Barone et al. (10 (link)). In short, glycosphingolipids were separated on aluminum-backed thin layer plates, and after drying the chromatograms were dipped for 1 min in diethylether/n-hexane (1:5, v/v) containing 0.5% (w/v) polyisobutylmethacrylate (Sigma-Aldrich) for 1 min. Thereafter, the chromatograms were soaked in PBS, pH 7.3, containing 2% bovine serum albumin and 0.1% NaN3 (solution A) for 2 h at room temperature. Suspensions of monoclonal antibodies (the dilutions used for each antibody are given in supplemental Table S2 ) were gently sprinkled over the chromatograms, followed by incubation for 2 h at room temperature. After washing with PBS followed a second 2-h incubation with 125I-labeled rabbit anti-mouse antibodies (DakoCytomation Norden A/S, Glostrup, Denmark) (labeled by the Iodogen method according to the manufacturer's (Pierce) instructions), diluted to 2 × 106 cpm/ml in solution A. Finally, the plates were washed six times with PBS. Dried chromatograms were autoradiographed for 12–24 h using XAR-5 x-ray films (Eastman Kodak).
The mouse monoclonal antibodies tested for binding to the acid glycosphingolipids of hESC in the chromatogram binding assay are given in
Acidic Glycosphingolipids
Aluminum
anti-H-2 antibodies
Antibodies
Biological Assay
Chloroform
Ethyl Ether
Glycosphingolipids
Human Embryonic Stem Cells
Immunoglobulins
Iodo-Gen
Mass Spectrometry
Methanol
Mice, House
Monoclonal Antibodies
n-hexane
p-anisaldehyde
Protons
Rabbits
resorcinol
Serum Albumin, Bovine
Silica Gel
Sodium Azide
Solvents
Technique, Dilution
Thin Layer Chromatography
X-Ray Film
Binding assays for ERα and ERβ were performed as previously described6 (link). Briefly, COS7 cells were transiently transfected with either ERα-GFP or ERβ-GFP). Following serum starvation for 24 h, cells (~5×104) were incubated with G-15 for 20 min. in a final volume of 10 μL prior to addition of 10 μL 20 nM E2-Alexa633 in saponin-based permeabilization buffer. Following 10 min at RT, cells were washed once with 200 μL PBS/2%BSA, resuspended in 20 μL and 2 μL samples were analyzed on a DAKO Cyan flow cytometers using HyperCyt™as described42 (link). For GPR30 binding, a radioiodinated derivative of G-1, 1-{2-[4-(6-Bromo-benzo[1,3]dioxol-5-yl)-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinolin-8-yl]-ethyl}-3-(3-iodo-phenyl)-urea, was used (see Supplementary Information , manuscript in preparation). Briefly, Hec50 cells were cultured in phenol-red free DMEM/F-12 containing 10% charcoal-stripped FBS, plated in 24-well tissue culture plates and grown to 80% confluence. Wells were rinsed with PBS and cells were incubated with competitor (G-1 or G15) for 30 minutes prior to addition of approximately 0.5-1 μCi of radioligand. The 125I radiolabeled ligand was prepared from the corresponding tributylstannane using Iodo-gen beads (Pierce) following the manufacturer’s recommended protocol. Complete details of the synthesis and radiolabeling will be described elsewhere (manuscript in preparation). Wells were incubated at 37°C for 1 hour, rinsed with PBS and radioactivity collected by ethanol extraction and counted in a Wallac Wizard 1480 gamma counter (Perkin Elmer, Gaithersburg, MD).
Anabolism
Biological Assay
Buffers
Cells
Charcoal
Ethanol
Gamma Rays
Iodine
Iodo-Gen
Ligands
Radioactivity
Saponin
Serum
Tissues
tributyltin
Urea
Anabolism
Biological Assay
Buffers
Cells
Charcoal
Ethanol
Gamma Rays
Iodine
Iodo-Gen
Ligands
Radioactivity
Saponin
Serum
Tissues
tributyltin
Urea
Anabolism
Biological Assay
Chimera
erbb2 Gene
Gel Chromatography
High-Performance Liquid Chromatographies
Iodo-Gen
Phosphates
Proteins
Radioactivity
Saline Solution
Serum Albumin, Bovine
Serum Albumin, Human
SGMIB
TERT protein, human
Thin Layer Chromatography
Trichloroacetic Acid
Tyrosine
VHH Immunoglobulin Fragments
Most recents protocols related to «Iodo-Gen»
68Ga-cyc-DX600 was prepared in house with DOTA-modified cyclic DX600 peptide (cyc-DX600-DOTA, DX600 peptide with condensed disulfide bond of cysteine) as the precursor following the reported protocol [11 (link), 12 ]. In detail, the newly eluted 68Ga3+ in 4 mL 0.05 M HCl was mixed with precursor in 1 mL 0.25 M NH4Ac, heated to 100 ℃ and maintained for 10 min. Radiochemical purity (RCP) was measured with HPLC system (1260 Infinity, Agilent Technologies) equipped with a radioactive detector (Flow-count, Eckert & Ziegler) to determine the labeling rate, as well as the stability in PBS and 5% fetal bovine serum for one hour incubation at room temperature.
18F-FDG was purchased from Atom Kexing Radiopharmaceuticals Ltd with strict quality control. Radiopharmaceuticals with labeling rate higher than 95% were used in imaging research immediately, and the specific radioactivity of 68Ga-cyc-DX600 was controlled as about 3.7 MBq/µg in the imaging research on various tumor-bearing mice models or patients.
To verify the maintain of ACE2 targeting ability on cellular level, 125I-labeled DX600 and 125I-labeled cyc-DX600-DOTA were synthesized via Iodogen-catalyzed iodization with I-125. Cellular binding was performed on 1 × 105 HEK-293T/hACE2 cells that expressed humanized ACE2 protein. After the co-culture with 1 nmol radiopharmaceuticals for 30 min or 1 h, the excess radiopharmaceuticals were washed away by cold PBS for three times, and the bound peptide or precursor was quantified with a gamma-detector.
18F-FDG was purchased from Atom Kexing Radiopharmaceuticals Ltd with strict quality control. Radiopharmaceuticals with labeling rate higher than 95% were used in imaging research immediately, and the specific radioactivity of 68Ga-cyc-DX600 was controlled as about 3.7 MBq/µg in the imaging research on various tumor-bearing mice models or patients.
To verify the maintain of ACE2 targeting ability on cellular level, 125I-labeled DX600 and 125I-labeled cyc-DX600-DOTA were synthesized via Iodogen-catalyzed iodization with I-125. Cellular binding was performed on 1 × 105 HEK-293T/hACE2 cells that expressed humanized ACE2 protein. After the co-culture with 1 nmol radiopharmaceuticals for 30 min or 1 h, the excess radiopharmaceuticals were washed away by cold PBS for three times, and the bound peptide or precursor was quantified with a gamma-detector.
ACE2 protein, human
Angiotensin Converting Enzyme 2
Cells
Coculture Techniques
Cold Temperature
Cyclic Peptides
Cystine
DX600 peptide
F18, Fluorodeoxyglucose
Fetal Bovine Serum
Gamma Rays
HEK293 Cells
High-Performance Liquid Chromatographies
Iodine-125
Iodo-Gen
Mus
Neoplasms
Patients
Peptides
Radioactivity
Radiopharmaceuticals
tetraxetan
Sar1, Ile8-AngII (30 µg in TRIS pH 7.5; 100 mM) was introduced in a tube coated with iodogen (ThermoFischer Scientific) with 0.4 mCi of Na125I (Perkin Elmer, Waltham, MA, USA, specific activity 17 Ci/mg, 0.1 M NaOH) for 20 min. After purification by HPLC and mass control with MALDI-TOF, the monoiodinated peptide was diluted in 10 mM HEPES supplemented with 1% bovine serum albumine (BSA).
Binding experiments were performed at room temperature using a mix of 100 μL of radioligand at 1 nM in 50 mM Tris HCl pH 7.4, 1 mM MgCl2, 0.1 g/L BSA, 0.3 μL of membranes of cells expressing receptors, and the competitor at different concentrations. Non-specific binding was determined in presence of 2 μM AngII. Filter plate (Unifilter−96 GF/C, Perkin Elmer) was saturated with polyethylenimine (PEI, 0.5%, Sigma Aldrich, Burlington, MA, USA). After 16 h of incubation at room temperature, samples were filtered and 25 μL of microscintillant (MicroScint-O, Perkin Elmer) were added to each dry filter before recording the radioactivity on the Packard TopCount counter (Perkin Elmer).
The toxins library was produced by the Venomics consortium [1 (link)]. The screening conditions (quantity of membranes, quantity of radioligand) were optimized beforehand to obtain a Z factor greater than 0.5, with Z = 1 − ((3 × MADmax + 3 × MADmin)/(medianmax − medianmin)), where MAD = Median absolute deviation. Eleven 96-well plates containing one toxin by well were screened. On each 96-well plate, eight wells were dedicated to total binding of the radioligand, and eight others were dedicated to non-specific binding. After counting the radioactivity bound in each well, peptides with an associated binding value less than Median – 3 × MAD were classified as hits.
Binding experiments were performed at room temperature using a mix of 100 μL of radioligand at 1 nM in 50 mM Tris HCl pH 7.4, 1 mM MgCl2, 0.1 g/L BSA, 0.3 μL of membranes of cells expressing receptors, and the competitor at different concentrations. Non-specific binding was determined in presence of 2 μM AngII. Filter plate (Unifilter−96 GF/C, Perkin Elmer) was saturated with polyethylenimine (PEI, 0.5%, Sigma Aldrich, Burlington, MA, USA). After 16 h of incubation at room temperature, samples were filtered and 25 μL of microscintillant (MicroScint-O, Perkin Elmer) were added to each dry filter before recording the radioactivity on the Packard TopCount counter (Perkin Elmer).
The toxins library was produced by the Venomics consortium [1 (link)]. The screening conditions (quantity of membranes, quantity of radioligand) were optimized beforehand to obtain a Z factor greater than 0.5, with Z = 1 − ((3 × MADmax + 3 × MADmin)/(medianmax − medianmin)), where MAD = Median absolute deviation. Eleven 96-well plates containing one toxin by well were screened. On each 96-well plate, eight wells were dedicated to total binding of the radioligand, and eight others were dedicated to non-specific binding. After counting the radioactivity bound in each well, peptides with an associated binding value less than Median – 3 × MAD were classified as hits.
cDNA Library
HEPES
High-Performance Liquid Chromatographies
Iodo-Gen
Magnesium Chloride
Peptides
Plasma Membrane
Polyethyleneimine
Radioactivity
Serum Albumin, Bovine
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tissue, Membrane
Toxins, Biological
Tromethamine
Direct iodination was investigated
with four oxidizing agents at pH 5 and pH 10. NMS (0.5 mg, 0.13 μmol)
was dissolved in 0.5 mL of PBS (pH 5 or pH 10) in a 1.5 mL LoBind
Eppendorf tube. Fifty nine micrograms (0.40 μmol, 3 equiv) of
sodium iodide, dissolved in 3.7 μL of PBS at pH 7.3, was added.
Four equivalents (0.53 μmol) of oxidation agents chloramine-T
(0.12 μg in 8.5 μL of PBS at pH 7.3), iodogen (0.23 μg
in 11.8 μL of PBS at pH 7.3), and freshly prepared chloramine
according to a published procedure24 (link) was
added. When using polymer-bound chloramine-T (loading: 0.2 mmol/g),
a single bead with a weight of 15 mg was used, which corresponds to
an amount of substance of about 3 μmol (22.7 equiv). The eight
samples were shaken at 22 °C by a horizontal rotation of 600
rpm. After 1 h, the samples were analyzed for their incorporation
of iodine by mass spectrometry.
with four oxidizing agents at pH 5 and pH 10. NMS (0.5 mg, 0.13 μmol)
was dissolved in 0.5 mL of PBS (pH 5 or pH 10) in a 1.5 mL LoBind
Eppendorf tube. Fifty nine micrograms (0.40 μmol, 3 equiv) of
sodium iodide, dissolved in 3.7 μL of PBS at pH 7.3, was added.
Four equivalents (0.53 μmol) of oxidation agents chloramine-T
(0.12 μg in 8.5 μL of PBS at pH 7.3), iodogen (0.23 μg
in 11.8 μL of PBS at pH 7.3), and freshly prepared chloramine
according to a published procedure24 (link) was
added. When using polymer-bound chloramine-T (loading: 0.2 mmol/g),
a single bead with a weight of 15 mg was used, which corresponds to
an amount of substance of about 3 μmol (22.7 equiv). The eight
samples were shaken at 22 °C by a horizontal rotation of 600
rpm. After 1 h, the samples were analyzed for their incorporation
of iodine by mass spectrometry.
chloramine-T
Iodides
Iodination
Iodine
Iodo-Gen
Mass Spectrometry
Oxidants
Polymers
The radioactive labeling was accomplished with 125I using the Iodogen method (52 (link)). Briefly, an Iodogen coated 0.5 mL microtube (Eppendorf, USA) was placed in 1 M phosphate buffer (pH 7.0), using 37 MBq [125I]-NaI (Isotop, Hungary) in 1 M NaOH and gently stirred for 5 min. Afterward, the labeling was done through the addition of 100 μg of C-PC dissolved in 100 μL of purified water. Then, the radiolabel was continued for an additional time of 20 min. The labeled C-PC was separated from the reaction medium in a Sephadex G25 column (GE Healthcare, USA) previously equilibrated in 1 M phosphate buffer (pH 7.0). Finally, the blue fractions with radiochemical purities of at least 90% were pooled and stored at 4°C until use. Blood samples (70 μL) were collected from the retro-orbital plexus by means of a heparinized capillary in anesthetized rats at 1, 15, and 30 min after the administration of 5 mg/kg C-PC. All samples were centrifuged at 10,000 rpm for 5 min. The 20µL plasma aliquot was added to 0.5 mL of 0.1% bovine serum albumin and 0.5 mL of 20% trichloroacetic acid. The insoluble material obtained by centrifugation at 10,000 rpm for 5 min (Eppendorf, Germany) was analyzed in a gamma counter (Berthold, Germany).
BLOOD
Buffers
Capillaries
Centrifugation
Gamma Rays
Iodo-Gen
Phosphates
Plasma
Radioactivity
Radiopharmaceuticals
Rattus
sephadex
Serum Albumin, Bovine
Trichloroacetic Acid
Chloramine-T trihydrate (Merck, Darmstadt, Germany), Copper(II)Sulphate, Penicillin, Streptomycin, RPMI-1640 (Sigma-Aldrich, Burlington, MA, USA), RPMI-1640 (Euroclone, Pero, Italy), DMEM low glucose (Sigma-Aldrich), Trypsin–EDTA (Sigma-Aldrich), Blasticidin hydrochloride (Sigma-Aldrich), Trichloroacetic acid (Merck), Fetal Bovine Serum (Merck, Darmstadt, Germany), Iodine 125 Radionuclide (Perkin Elmer, Waltham, Mass., USA), Iodogen™ iodination reagent (Pierce, Thermo-Fischer), Alexa-488 succinimidyl ester (Thermo Fischer Scientific, Waltham, Mass., USA), Anti-CD146 microbeads, anti-F4/80 microbeads, anti-CD 11b microbeads (Miltenyi Biotech, Bergisch Gladbach, Germany), HSA Alburex (CSL Behring, King of Prussia, Penn., USA), Fetal Bovine Serum (Biowest, Nuialle, France), Resazurin (biotechne, Minneapolis, Minn., USA), Liberase™TM (Roche, Basel, Switzerland), Human fibronectin was extracted from expired human plasma donated from the hospital (University Hospital of Northern Norway, Tromsø, Norway) blood-bank, by affinity chromatography locally, using the method of Vuento 197961 (link), Formaldehyde treated Serum Albumin (FSA) was prepared as described in Mego 196762 (link), Blomhoff 198432 (link), AGE-BSA was prepared as described in Hansen 200250 (link), Oxidized Low Density Lipoprotein (oxLDL) was prepared by Copper Sulphate oxidation as previously described in Li 201135 (link).
advanced glycation end products-bovine serum albumin
chloramine-T trihydrate
Chromatography, Affinity
Copper
Edetic Acid
Esters
Fetal Bovine Serum
Fibronectins
formaldehyde-serum albumin
Glucose
Homo sapiens
Iodination
Iodine Radioisotopes
Iodo-Gen
Liberase
Microspheres
oxidized low density lipoprotein
Penicillins
Plasma
resazurin
Streptomycin
Sulfate, Copper
Sulfates, Inorganic
Trichloroacetic Acid
Trypsin
Top products related to «Iodo-Gen»
Sourced in United States, France
Iodogen is a laboratory reagent used for the iodination of proteins. It is a non-radioactive, mild oxidizing agent that can be used to incorporate radioactive iodine into proteins, peptides, or other molecules. Iodogen facilitates the labeling process by catalyzing the iodination reaction, allowing for the efficient attachment of iodine isotopes to target compounds.
Sourced in United States, United Kingdom, Germany, Sweden, Japan, Canada, Belgium
The PD-10 column is a size-exclusion chromatography column designed for desalting and buffer exchange of protein samples. It is commonly used to separate low molecular weight substances from high molecular weight compounds, such as proteins, in a rapid and efficient manner.
Sourced in United States
Iodogen is a lab equipment product manufactured by Merck Group. It is a reagent used for the iodination of proteins and peptides. Iodogen functions as an oxidizing agent to facilitate the covalent attachment of iodine to tyrosine residues within target molecules.
Sourced in United States
Na125I is a radioactive isotope of sodium that is used as a tracer in various laboratory applications. It emits gamma radiation, which can be detected and measured to provide information about the behavior and distribution of the labeled compounds or samples.
Iodogen pre-coated tubes are a type of laboratory equipment used for the iodination of proteins. The tubes are pre-coated with a reagent called Iodogen, which facilitates the covalent labeling of proteins with radioactive iodine isotopes. This process is commonly employed in various research applications, such as the study of protein-protein interactions and the preparation of labeled proteins for immunoassays.
Sourced in United States
The BioSpin Tris Columns are spin columns used for the purification and concentration of biomolecules, such as proteins and nucleic acids, from complex biological samples. These columns are packed with a specialized resin that selectively binds and retains the target biomolecules, allowing for the removal of contaminants and impurities through a simple centrifugation process.
Sourced in United States, United Kingdom, Sweden, Germany, Denmark, China, Switzerland, Belgium, Japan
The PD-10 desalting column is a laboratory equipment used for the separation and purification of biomolecules. It functions by removing salts, buffer components, or other small molecular weight substances from protein or nucleic acid samples, allowing for the recovery of the desired macromolecules in a purified form.
Sourced in Panama
Non-specific mouse IgG is a purified antibody preparation derived from mouse serum. It serves as an isotype-matched control for experiments utilizing mouse monoclonal antibodies.
Sourced in Sweden, United States
Iodine-125 is a radioisotope used in various laboratory and medical applications. It has a half-life of approximately 60 days and emits low-energy gamma rays. Iodine-125 is commonly used in radioactive tracer studies, radioimmunoassays, and other analytical techniques.
Sourced in United Kingdom, United States, Japan
The PD MiniTrap G-25 column is a pre-packed size exclusion chromatography column designed for desalting and buffer exchange of small molecules and peptides. It is made of inert materials and has a total bed volume of 5 mL.
More about "Iodo-Gen"
Iodogen, also known as Iodo-Gen, is a versatile reagent commonly used in the iodination of proteins and other macromolecules.
It is a mild, water-soluble oxidizing agent that can be employed to label a variety of compounds with radioactive iodine, such as tyrosine and histidine residues in proteins.
This technique is particularly useful in immunoassays, receptor binding studies, and other applications where radiolabeled compounds are required.
The Iodogen method offers several advantages over alternative iodination techniques.
It provides improved labeling efficiency and utilizes milder oxidation conditions, which helps preserve the biological activity of the labeled molecule.
This makes Iodogen a popular choice among researchers and scientists.
Iodogen can be used in conjunction with various related products and techniques, including PD-10 columns for desalting and purification, Na125I for the radioactive iodine source, and Iodogen pre-coated tubes for a convenient iodination protocol.
Additionally, BioSpin Tris Columns and PD MiniTrap G-25 columns can be used for further purification and desalting of the iodinated samples.
When working with Iodogen, it's important to consider factors such as reaction time, temperature, and the ratio of Iodogen to the target molecule to optimize the labeling process.
Researchers may also need to use non-specific mouse IgG as a carrier protein or to block non-specific binding during the iodination and subsequent assays.
Overall, Iodogen's versatility, mild reaction conditions, and ability to preserve biological activity make it a valuable tool in a wide range of research applications involving the iodination of proteins and other macromolecules.
By understanding the related products and techniques, researchers can leverage the power of Iodogen to enhance their experimental designs and achieve reliable, reproducible results.
It is a mild, water-soluble oxidizing agent that can be employed to label a variety of compounds with radioactive iodine, such as tyrosine and histidine residues in proteins.
This technique is particularly useful in immunoassays, receptor binding studies, and other applications where radiolabeled compounds are required.
The Iodogen method offers several advantages over alternative iodination techniques.
It provides improved labeling efficiency and utilizes milder oxidation conditions, which helps preserve the biological activity of the labeled molecule.
This makes Iodogen a popular choice among researchers and scientists.
Iodogen can be used in conjunction with various related products and techniques, including PD-10 columns for desalting and purification, Na125I for the radioactive iodine source, and Iodogen pre-coated tubes for a convenient iodination protocol.
Additionally, BioSpin Tris Columns and PD MiniTrap G-25 columns can be used for further purification and desalting of the iodinated samples.
When working with Iodogen, it's important to consider factors such as reaction time, temperature, and the ratio of Iodogen to the target molecule to optimize the labeling process.
Researchers may also need to use non-specific mouse IgG as a carrier protein or to block non-specific binding during the iodination and subsequent assays.
Overall, Iodogen's versatility, mild reaction conditions, and ability to preserve biological activity make it a valuable tool in a wide range of research applications involving the iodination of proteins and other macromolecules.
By understanding the related products and techniques, researchers can leverage the power of Iodogen to enhance their experimental designs and achieve reliable, reproducible results.