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F8630

Sigma-Aldrich

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

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

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

UniProt accession no.

storage temp.

−20°C

Gene Information

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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

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.

Reconstitution

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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
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
Yuya Nakatani et al.
Archives of oral biology, 73, 172-178 (2016-10-25)
Platelet-rich plasma (PRP) is typically isolated and applied immediately after preparation, making it both a time- and labor-intensive addition to the operative procedure. Thus, it would be convenient if PRP could be preserved. We evaluated the efficacy of freeze-dried PRP
Ying Chen et al.
Cell discovery, 3, 17046-17046 (2017-12-22)
The capacity of digit tip regeneration observed both in rodents and humans establishes a foundation for promoting robust regeneration in mammals. However, stimulating regeneration at more proximal levels, such as the middle phalanges (P2) of the adult mouse, remains challenging.
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

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