Angiotensin 1

Manufactured by Bruker

Sourced in United States

Angiotensin I is a peptide hormone used in laboratory research. It is a precursor to the potent vasoconstrictor angiotensin II. Angiotensin I is used in various biochemical and physiological studies, but a detailed description of its core function is not available while maintaining an unbiased and factual approach.

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Lab products found in correlation

Angiotensin 2, by Bruker (4 mentions) Bombesin, by Bruker (4 mentions) Acth clip 1 17, by Bruker (4 mentions) Acth clip 18 39, by Bruker (4 mentions) Somatostatin 28, by Bruker (3 mentions) Substance p, 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) Epicatechin, by Fujifilm (1 mentions) Afzelechin, by ChemFaces (1 mentions) Cmc sodium salt, by Fujifilm (1 mentions) Indium tin oxide coated glass slides 100 ω without mas coating, by Matsunami (1 mentions) Catechin, by Fujifilm (1 mentions) Acetone, by Avantor (1 mentions) Isopropanol, by Avantor (1 mentions)

5 protocols using angiotensin 1

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 of Polyphenols

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(+)-Catechin, (−)-epicatechin, CMC sodium salt, methanol, and water were purchased from Wako Chemicals (Tokyo, Japan). (+)-Afzelechin was purchased from ChemFaces (Wuhan, China). Procyanidin B1 and procyanidin B2 were purchased from Funakoshi Co. (Tokyo, Japan). Procyanidin C1 and cinnamtannin A2 were purchased from Kanto Chemical Co. (Tokyo, Japan). CHCA, 9AA, and DAN were purchased from Tokyo Kasei Co. (Tokyo, Japan). Indium-tin-oxide (ITO)-coated glass slides (100 Ω without MAS coating) were purchased from Matsunami Glass (Osaka, Japan). Peptide calibration stndards containing bradykinin (1–7), angiotensin II, and angiotensin I were purchased from Bruker (Billerica, MA, USA). All reagents and solvents used in this study were of analytical grade.

Enomoto H., Takahashi S., Takeda S, & Hatta H. (2019). Distribution of Flavan-3-ol Species in Ripe Strawberry Fruit Revealed by Matrix-Assisted Laser Desorption/Ionization-Mass Spectrometry Imaging. Molecules, 25(1), 103.

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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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