Description_x000D_ Amino Acid Sequence_x000D_ Glu-Gly-Val-Asn-Asp-Asn-Glu-Glu-Gly-Phe-Phe-Ser-Ala-Arg_x000D_ General description_x000D_ Fibrinopeptide B (FPB) is produced during the cleavage of fibrinogen, by thrombin, to fibrin monomer. It is cleaved off from the N-terminal of the fibrinogen β chain. This peptide is composed of 14 amino acids._x000D_ Application_x000D_ [Glu1]-Fibrinopeptide B human has been used:_x000D_ • during LC-MS to avoid cross-contamination and to analyze the performance of mass spectrometer and LC-instrument_x000D_ • for two-point calibration during 2D (dimensional) gel electrophoresis and protein identification by mass spectrometry of histidine (his)-Pup (prokaryotic ubiquitin-like protein) isolated from Mycobacterium smegmatis_x000D_ • for two-point calibration during one-dimensional gel electrophoresis and tandem mass spectrometry (MS) for the characterization of soluble protein sample obtained from the salivary gland homogenates of Cimex lectularius_x000D_ • as a standard for the correction of mass drift in data obtained from MS and MS/MS performed on peptides obtained from trypsin-digestion of protein disulfide isomerase (PDI)_x000D_ Biochem/physiol Actions_x000D_ Fibrin formation is an essential part in wound healing and inflammation. Fibrinopeptide B (FPB) can also cause chemotactic migration of neutrophils, without the simultaneous release of lysosome enzymes. It is produced during the coagulation of fibrinogen, which is essential for physiological homeostasis. It is involved in various disorders such as thrombosis and disseminated intravascular coagulation._x000D_ Other Notes_x000D_ Lyophilized from 0.1% TFA in H2O