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Fibrinopeptide b

Manufactured by Merck Group

Fibrinopeptide B is a lab equipment product. It is a protein fragment that is released during the conversion of fibrinogen to fibrin, which is a key step in the blood clotting process. The core function of Fibrinopeptide B is to facilitate the monitoring and analysis of this blood clotting mechanism in a laboratory setting.

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2 protocols using fibrinopeptide b

1

Antibody and Protein Characterization Protocol

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IgGs utilized were SILu (Sigma MSQC4) and anti-BNP (ICL RBNP-65A-Z). All other proteins were purchased from Sigma-Aldrich: bovine serum albumin (BSA; A7906), human haptoglobin (H3536), bovine carbonic anhydrase (C2624), bovine myoglobin (M5696), bovine α-lactalbumin (L5385), and bovine ubiquitin (U6253). Peptides utilized were a custom peptide (H-GLFYVDFLSQDKV-SIALSSHWINPR-OH, 2894.29 Da; Global Peptide), fibrinopeptide B (1570.6 Da; Sigma F3261), and Z-Leu-Leu-Leu-al (475.62 Da; Sigma C2211). Detergents were purchased from Sigma-Aldrich: CHAPS (3-[(3-Cholamidopropyl)-dimethylammonio]-1-propanesulfonate hydrate; C3023) and Triton X-100 (X-100). Chromatography solvents were purchased from Fisher: water (Optima LC/MS grade; W64), acetonitrile (Optima LC/MS grade; A9554), and formic acid (Pierce LC/MS grade; PI28905).
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2

MALDI-TOF Mass Spectrometry Protocol

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MALDI-TOF spectra were recorded by either a Voyager DE-STRTM MALDI–TOF or a 4800 MALDI-TOF/TOF mass spectrometer (Applied Biosystems, Darmstadt, Germany) with MALDI-TOF/TOF spectra acquired with the latter instrument. The 4700 Calibration standard kit (Applied Biosystems) was used for calibrating the MS mode and fibrinopeptide B (Sigma) was used for calibrating the MS/MS mode. The collision energy for MS/MS was set to 1 kV, and the collision gas was argon. 2, 5-Dihydroxybenzoic acid and 3,4-diaminobenzophenone were used as matrix. Permethylated samples were dissolved in methanol (10 μL) and the solution premixed with matrix (20 mg/mL) with a ratio of 1:1 (v/v) with the mixture (1 μL) being spotted on the plate.
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