Angiotensin 2

Manufactured by Bruker

Sourced in United States

Angiotensin II is a peptide hormone that plays a key role in the regulation of blood pressure and fluid balance in the body. It is a product offered by Bruker for use in laboratory research and analysis.

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Lab products found in correlation

Bombesin, by Bruker (5 mentions) Acth clip 18 39, by Bruker (5 mentions) Angiotensin 1, by Bruker (4 mentions) Acth clip 1 17, by Bruker (4 mentions) Somatostatin 28, by Bruker (3 mentions) Substance p, by Bruker (2 mentions) Bradykinin 1 7, by Bruker (2 mentions) Fleximaging, by Bruker (1 mentions) Flexcontrol, by Bruker (1 mentions) Methanol, by Carl Roth (1 mentions) Voyager de str matrix, by Thermo Fisher Scientific (1 mentions) Angiotensin1, by Thermo Fisher Scientific (1 mentions) Des argbradykinin, by Thermo Fisher Scientific (1 mentions) Ultraflex mass spectrometer, by Bruker (1 mentions) Acetone, by Avantor (1 mentions) Isopropanol, by Avantor (1 mentions) Bovine insulin, by Merck Group (1 mentions) Mcf 7 cell, by American Type Culture Collection (1 mentions) Fetal bovine serum (fbs), by American Type Culture Collection (1 mentions) Eagle s minimum essential medium emem, by American Type Culture Collection (1 mentions)

6 protocols using angiotensin 2

MALDI-MSI of Peptide Tissue Profiles

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MSI was performed using a RapifleX MALDI Tissuetyper time-of-flight (TOF) mass spectrometer (Bruker Daltonics). A peptide calibration standard mix (bradykinin, angiotensin II, angiotensin I, substance P, bombesin, ACTH clip 1–17, ACTH clip 18–39, and somatostatin 28 (Bruker Daltonics)) was used for external calibration. Each spectrum was automatically generated at a spatial resolution of 50 µm using flexControl (Bruker Daltonics) in the mass range of m/z = 600–3200. 500 laser shots were acquired for each spectrum at 1 kHz, with a laser power of 65–80%. The measurement regions were defined using flexImaging (Bruker Daltonics). Following the MSI measurements, matrix was removed by two washes in 99.99% methanol (Carl Roth GmbH, Karlsruhe, Germany) for 2 min each, followed by two washings in 99.99% ethanol (Carl Roth GmbH) for 10 s.

Gonçalves J.P., Bollwein C., Schlitter A.M., Martin B., Märkl B., Utpatel K., Weichert W, & Schwamborn K. (2021). The Impact of Histological Annotations for Accurate Tissue Classification Using Mass Spectrometry Imaging. Metabolites, 11(11), 752.

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MALDI-TOF Mass Spectrometry Protocol

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Mass spectra were acquired in positive linear or reflector mode using either a Voyager DE STR matrix-assisted laser desorption ionisation mass spectrometer (Applied Biosystems, Warrington, UK) or a Bruker Ultraflex mass spectrometer (Bruker Daltonic GmbH, Bremen, Germany). Samples were mixed with equal volumes of either α-Cyano-4-hydroxycinnamic acid (10 mg/ml in 70% acetonitrile, 0.1% TFA) or 2,5-Dihydroxybenzoic acid (10 mg/ml in 20% acetonitrile, 1% formic acid) on the MALDI sample plate and allowed to air-dry.
External calibration was conducted using a calibration mixture containing des-Argbradykinin, angiotensin1, Glu-fibrinopeptide B, and neurotensin (Applied Biosystems) or angiotensin I, angiotensin II, substance P, bombesin, ACTH clip 1-17 , ACTH clip 18-39 and somatostatin 28 (Bruker Daltonics). Masses are shown as average masses [M+H] + for analyses performed in linear mode and monoisotopic masses for analyses in reflector mode.

Sturm S., Dowle A., Audsley N, & Isaac R.E. (2020). The structure of the Drosophila melanogaster sex peptide: Identification of hydroxylated isoleucine and a strain variation in the pattern of amino acid hydroxylation. Insect biochemistry and molecular biology, 124.

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MALDI-TOF Mass Spectrometry Proteomics Protocol

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MALDI-TOF MS was performed using an autoflex MALDI reflectron TOF mass spectrometer (Bruker Daltonics) as describe previously [14] (link). Each sample (0.5 mL, representing ∼5% of the total digest volume) was mixed with 0.5 mL of the matrix (CHCA, 10 mg/mL in 50% ACN/0.1% TFA), spotted onto the MS plate, and air dried. The samples were analyzed by MALDI-TOF MS operating in the delayed extraction/reflectron/positive ion detection mode with an accelerating voltage of 15 kV and a 499 ns delay. A nitrogen laser (337 nm) was used to irradiate the sample, and a mass spectrum was acquired in the mass range 800–3,000 Da. The instrument was externally calibrated using five peptide standards (MH1: Angiotensin II, 1046.5420 Da; Angiotensin I, 1296.6853 Da; Substance P, 1347.7361 Da; Bombesin, 1619.823 Da; and ACTH clip 18–39, 2465.199 Da) from Bruker or internally calibrated with autodigest peaks of trypsin (MH1: 2163.057 Da, 2273.160 Da). ACTH was also used as an internal lock mass at m/z 2465.199 when added to the matrix at 100 fmol/mL.

Li W., Wang W., Li Y., Wang W., Wang T., Li L., Han Z., Wang S., Ma D, & Wang H. (2014). Proteomics Analysis of Normal and Senescent NG108-15 Cells: GRP78 Plays a Negative Role in Cisplatin-Induced Senescence in the NG108-15 Cell Line. PLoS ONE, 9(3), e90114.

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Quantitative Proteomic Analysis of MCF-7 Cells

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MCF-7 cells, eagle’s minimum essential medium (EMEM), and fetal bovine serum were obtained from ATCC (USA). Dulbecco’s phosphate-buffered saline (DPBS) buffer and the Hausser scientific hemocytometer were purchased from Thermo Fisher Scientific (USA). Acetonitrile, alpha-cyano-4-hydroxycinnamic acid (α-CHCA), human Bcl-2, anti-Bcl-2 antibody, bovine serum albumin (BSA), and bovine insulin were purchased from Sigma-Aldrich (USA). The peptide calibration mixture (angiotensin II 1046.5418 m/z [M+H]⁺, angiotensin I 1296.6848 m/z [M+H]⁺, substance P [1347.7354 m/z [M+H]⁺, bombesin 1619.8223 m/z [M+H]⁺, ACTH clip 1-17 2093.0862 m/z [M+H]⁺, ACTH clip 18-39 2465.1983 m/z [M+H]⁺, and somtostatin-28 3147.4710 m/z [M+H]⁺) was purchased from Bruker Daltonics Inc (USA). Isotope labeled peptides (FATVVEEL(d10)FR and FATVVEEL(13C15N)FR) were purchased from GenScript USA Inc. Polydimethylsiloxane (PDMS) was purchased from Dow Corning Corporation (USA). Indium tin oxide (ITO) coated glass slides (100 ohm/sq) were obtained from NANOCS (USA). Cr was obtained from SPI Supplies (USA). Tridecafluoro-1, 1, 2, 2-tetra-trichlorosilane (TTTS) was purchased from Gelest (USA). Isopropanol and acetone were from VWR (USA). SU-8 2075 photoresist and SU-8 developer were from MicroChem (USA). Ultrapure water was supplied from a synergy purification system (Millipore, USA).

Yang M., Villarreal J.C., Ariyasinghe N., Kruithoff R., Ros R, & Ros A. (2021). A quantitative approach for protein analysis in small cell ensembles by an integrated microfluidic chip with MALDI mass spectrometry. Analytical chemistry, 93(15), 6053-6061.

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MALDI-TOF Mass Spectrometry Protocol

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Mass spectra were acquired in positive reflector mode using Bruker ultrafleX III or ultrafleXtreme mass spectrometers (Bruker Daltonics, Bremen, Germany). Samples were mixed with 0.5 µl 2,5-Dihydroxybenzoic acid (DHB, 10 mg/ml in 20% acetonitrile, 1% FA) on the MALDI sample plate and dried using a gentle stream of hot air. External calibration was conducted using calibration mixtures containing bradykinin 1-7 , angiotensin I, angiotensin II, substance P, bombesin, ACTH clip 1-17 , ACTH clip 18-39 , somatostatin 28, insulin and ubiquitin I (Bruker Daltonics).

Sturm S., Dowle A., Audsley N, & Isaac R.E. (2021). Mass spectrometric characterisation of the major peptides of the male ejaculatory duct, including a glycopeptide with an unusual zwitterionic glycosylation. Journal of proteomics, 246.

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MALDI-TOF MS Calibration Standards

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Water, methanol, potassium acetate, and formic acid were purchased from FUJIFILM Wako Pure Chemical Corp. (Tokyo, Japan). In addition, 2,5-dihydroxybenzoic acid (DHB) and α-cyano-4-hydroxycinnamic acid (CHCA) were purchased from Tokyo Kasei Kogyo Co., Ltd. (Tokyo, Japan). Peptide calibration standards, namely bradykinin (1–7) and angiotensin II, were purchased from Bruker Corp. (Billerica, MA, USA). All reagents and solvents used in the study were of analytical grade.

Enomoto H., Furukawa T., Takeda S., Hatta H, & Zaima N. (2020). Unique Distribution of Diacyl-, Alkylacyl-, and Alkenylacyl-Phosphatidylcholine Species Visualized in Pork Chop Tissues by Matrix-Assisted Laser Desorption/Ionization–Mass Spectrometry Imaging. Foods, 9(2), 205.

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