F8630
Fibrinogen from bovine plasma
Type I-S, 65-85% protein (≥75% of protein is clottable)
Synonym(s):
Factor I
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About This Item
Form:
powder
Biological source:
bovine plasma
Mol wt:
α-chain 63.5 kDa, β-chain 56 kDa, γ chain 47 kDa (about 4% carbohydrate content), soluble dimer 340 kDa
biological source
bovine plasma
type
Type I-S
form
powder
mol wt
α-chain 63.5 kDa, β-chain 56 kDa, γ chain 47 kDa (about 4% carbohydrate content), soluble dimer 340 kDa
concentration
65-85% (biuret)
technique(s)
cell culture | mammalian: suitable
storage temp.
−20°C
Quality Level
Gene Information
cow ... FGA(522039), FGB(510522), FGG(280792)
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Application
Fibrinogen has been used in studies of haemostatic therapy in surgical and massive trauma patients. These studies have shown that fibrinogen may prove to be more superior in stopping blood loss when compared to using fresh frozen plasma (FFP).
Biochem/physiol Actions
Acute phase protein that is part of the coagulation cascade of proteins.
Fibrinogen is an acute phase protein that is part of the coagulation cascade of proteins. The end result of the cascade is the production of thrombin that converts fibrinogen to fibrin. Thrombin rapidly proteolyzes fibrinogen, releasing fibrinopeptide A. The loss of this small peptide is not sufficient to make the resulting fibrin molecule insoluble, but it tends to form complexes with adjacent fibrin and fibrinogen molecules. Thrombin then cleaves a second peptide, fibrinopeptide B, from fibrin and the fibrin monomers formed then polymerize spontaneously to form an insoluble gel. The polymerized fibrin is held together by noncovalent and electrostatic forces and stabilized by the transamidating enzyme, factor XIIIa, that is produced by the action of thrombin on factor XIII. The insoluble fibrin aggregates (clots) and aggregated platelets then block the damaged blood vessel and prevent further bleeding. The amount of fibrinogen in the plasma can serve as a nonspecific indicator of whether or not an inflammatory process is present in the body. Fibrinogen from any mammalian source will be cleaved by thrombin from any mammalian source.
Physical form
Contains ~10% sodium citrate and ~15% sodium chloride.
Preparation Note
The optimal way to solubilize fibrinogen is to layer it on top of warm (37 ºC) saline, as fibrinogen will not dissolve in water. The saline concentration can be in the range of 0.85-0.9%. The fibrinogen-saline solution can be gently agitated, but it must not be vortexed. The fibrinogen will slowly dissolve to give a hazy solution. Fibrinogen may be sterile-filtered, but may not go through a 0.1 μm filter. A 0.2 μm filter is suggested, with positive pressure using a syringe and "button" filter. Vacuum filtration should not be used, since this will lead to breakdown of the molecule during the filtration.
Analysis Note
Protein determined by biuret
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Katarzyna Kubiak et al.
Colloids and surfaces. B, Biointerfaces, 139, 123-131 (2015-12-27)
Adsorption kinetics of fibrinogen at a gold substrate at various pHs was thoroughly studied using the QCM-D method. The experimental were interpreted in terms of theoretical calculations performed according to the random sequential adsorption model (RSA). In this way, the
C Fenger-Eriksen et al.
British journal of anaesthesia, 101(6), 769-773 (2008-09-27)
Patients experiencing massive haemorrhage are at high risk of developing coagulopathy through loss, consumption, and dilution of coagulation factors and platelets. It has been reported that plasma fibrinogen concentrations may reach a critical low level relatively early during bleeding, calling
Johanna Prüller et al.
PloS one, 13(9), e0202574-e0202574 (2018-09-18)
Biophysical/biochemical cues from the environment contribute to regulation of the regenerative capacity of resident skeletal muscle stem cells called satellites cells. This can be observed in vitro, where muscle cell behaviour is influenced by the particular culture substrates and whether
Sunghoon Lee et al.
Nature nanotechnology, 14(2), 156-160 (2019-01-02)
In biointegrated electronics, the facile control of mechanical properties such as softness and stretchability in electronic devices is necessary to minimize the perturbation of motions inherent in biological systems1-5. For in vitro studies, multielectrode-embedded dishes6-8 and other rigid devices9-12 have
Navid Hakimi et al.
Lab on a chip, 18(10), 1440-1451 (2018-04-18)
We present a handheld skin printer that enables the in situ formation of biomaterial and skin tissue sheets of different homogeneous and architected compositions. When manually positioned above a target surface, the compact instrument (weight <0.8 kg) conformally deposits a
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