Glu1 fibrinopeptide

Manufactured by Merck Group

Sourced in Germany, United States

[glu1]-fibrinopeptide is a laboratory reagent used in various scientific research applications. It is a synthetic peptide fragment derived from the human fibrinogen protein. The primary function of [glu1]-fibrinopeptide is to serve as a standard or control substance for assays and analytical procedures involving fibrinogen or related proteins.

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Lab products found in correlation

Adrenocorticotropic hormone, by Merck Group (1 mentions) Angiotensin 2, by Merck Group (1 mentions) Bradykinin fragment 1 7, by Merck Group (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Sodium chloride (nacl), by Thermo Fisher Scientific (1 mentions) Ammonium hydroxide, by Thermo Fisher Scientific (1 mentions) Sodium bicarbonate, by Thermo Fisher Scientific (1 mentions) Acetonitrile with 0.1 formic acid, by Thermo Fisher Scientific (1 mentions) Hplc grade water, by Thermo Fisher Scientific (1 mentions) Zwittergent 3 12, by Merck Group (1 mentions) Calcium chloride, by Merck Group (1 mentions)

Close spelling variants of this product

[Glu1] fibrinopeptide B human (9 citations) [Glu1]‐fibrinopeptide B (8 citations) Glu1]-Fibrinopeptide B human (Glufib) (2 citations)

2 protocols using glu1 fibrinopeptide

Mass Spectrometry of Biological Peptides

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Water was double distilled using quartz apparatus from Heraeus Quarzschmelze (Hanau, Germany). Acetonitrile, glycine (Gly), and leucine (Leu) were bought from PENTA (Praha, Czech Republic). Trifluoroacetic acid (TFA), α-cyano-4-hydroxycinnamic acid (CHCA), ammonium bicarbonate (ABC), 3,5 dimethoxy-4-hydroxycinnamic acid (sinapinic acid, SA), tryptophan (Trp), and bovine serum albumin (BSA) were purchased from Sigma-Aldrich (Steinheim, Germany). Black phosphorus was purchased from Chempur (Karlsruhe, Germany). Phenylalanine (Phe) was purchased from Merck (Darmstadt, Germany). Bradykinin fragment 1–7, angiotensin II, [glu¹]-fibrinopeptide, adrenocorticotropic hormone [1–17] (ACTH [1–17]), and adrenocorticotropic hormone [18–39] (ACTH [18–39]) were purchased from Sigma-Aldrich (Steinheim, Germany). Humanin peptides A (C₈₄H₁₃₈N₂₀O₂₄S, PRGFSCLLLLTGEIDLP), B (C₈₃H₁₃₆N₂₀O₂₃S₂, PRGFSCLLLLCGEIDLP), C (C₈₅H₁₄₀N₂₀O₂₅S, PRGFSCLLLLTSEIDLP), and D (C₁₁₈H₂₀₂N₃₄O₃₁S₂, MAPRGFSCLLLLTGEIDLPVKRRA) were purchased from Clonestar biotech (Brno, Czech Republic). CCTL14 line of hESC [46, XX] registered in Human Pluripotent Stem Cell Registry was used in this study. This hESC line was kindly provided by Dr. Aleš Hampl, Ph.D. from the Department of Histology and Embryology, Faculty of Medicine, Masaryk University, and used in consonance with the official permission (MSMT-14648/2016-5).

Mandal G., Moráň L., Pečinka L., Vaňhara P, & Havel J. (2022). Matrix enrichment by black phosphorus improves ionization and reproducibility of mass spectrometry of intact cells, peptides, and amino acids. Scientific Reports, 12, 1175.

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Quantitative Analysis of Apolipoproteins

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Tris, ammonium hydroxide, sodium chloride, sodium bicarbonate, HPLC grade water and acetonitrile with 0.1% formic acid were purchased from Fisher Scientific (Fair Lawn, NJ, U.S.A.). Zwittergent 3–12 was purchased from EMD Millipore (Billerica, MA, U.S.A.). Calcium chloride and [Glu1]-Fibrinopeptide were purchased from Sigma-Aldrich (St. Louis, MO, U.S.A.). The IMER column, digestion and wash buffers were obtained from Perfinity Biosciences (West Lafayette, IN, U.S.A.). Protein standard materials, apoA-II, apoC-I, apoC-II and apoC-III were obtained from Academy Bio-Medical (Houston, Texas, U.S.A.). ApoA-IV and apoE were obtained from Novoprotein Scientific (Summit, NJ, U.S.A.). All protein standards were ≥98% pure, based on SDS-PAGE performed by the manufacturer, and were used without further purification. The concentrations of the protein stock solutions prepared from these solid materials were confirmed by amino acid analysis performed by Midwest Bio-Tech. (Fishers, IN, U.S.A.).

Toth C.A., Kuklenyik Z., Jones J.I., Parks B.A., Gardner M.S., Schieltz D.M., Rees J.C., Andrews M.L., McWilliams L.G., Pirkle J.L, & Barr J.R. (2016). On-column trypsin digestion coupled with LC-MS/MS for quantification of apolipoproteins. Journal of proteomics, 150, 258-267.

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