Merck
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F4883

Sigma-Aldrich

Fibrinogen from human plasma

35-65% protein (≥90% of protein is clottable).

Synonym(s):
Factor I
CAS Number:
EC Number:
MDL number:
NACRES:
NA.32

biological source

human plasma

Quality Level

description

essentially plasmin(ogen) free

form

powder

quality

35-65% protein (≥90% of protein is clottable).

mol wt

α-chain 63.5 kDa
β-chain 56 kDa
γ chain 47 kDa (about 4% carbohydrate content)
soluble dimer 340 kDa

concentration

35-65% protein (biuret)

technique(s)

cell culture | mammalian: suitable

solubility

0.9% NaCl: soluble

UniProt accession no.

storage temp.

−20°C

Gene Information

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This Item
F8630341576-M341573
form

powder

form

powder

form

lyophilized

form

lyophilized

mol wt

α-chain 63.5 kDa, β-chain 56 kDa, γ chain 47 kDa (about 4% carbohydrate content), soluble dimer 340 kDa

mol wt

α-chain 63.5 kDa, β-chain 56 kDa, γ chain 47 kDa (about 4% carbohydrate content), soluble dimer 340 kDa

mol wt

-

mol wt

-

concentration

35-65% protein (biuret)

concentration

65-85% (biuret)

concentration

-

concentration

-

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

-

solubility

0.9% NaCl: soluble

solubility

-

solubility

sterile distilled water: soluble

solubility

sterile distilled water: soluble

General description

Fibrinogen was the first blood coagulation factor to be identified, and it is a precursor of fibrin protein. This protein is composed of two chains, each of which is composed of three chains- α, β and γ. These three subunits are coded by three genes located in the human chromosomal locus 4q23-q32, and spans 51kb.

Application

Fibrinogen from human plasma has been used for-
  • fibrinogen adsorption assay performed on swCNTs (single-walled carbon nanotubes)
  • the characterization of fibrinogen structure in the presence of CNT using CD (Circular dichroism) spectroscopy and temperature scan
  • the preparation of RBC suspension obtained from venous blood of antecubital vein, to assess RBC aggregability
  • fibrinolysis assay performed on mouse embryonic fibroblasts (MEFs)
  • the preparation of fibrinogen-labeled gold (Fgn/Au)
  • the quantification of in vitro angiogenesis by human microvascular endothelial cells and
  • the assessment of fibrin-induced apoptosis and differentiation-regulation in trophoblast obtained from term human placentas.

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 proteolyses 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.
Fibrinogen is an acute-phase inflammatory protein, which plays an essential role in blood clotting. Coronary heart disease is linked to the plasma levels of fibrinogen in Chinese population, and might have potential as a marker and risk factor for the same. A -455 allele of fibrinogen β (FGB) chain is linked with poor survival in Caucasian women with Finnish stroke. Ischemic stroke preceded by hyperfibrinogenemia has poor outcome, which is independent of the baseline fibrinogen concentration.

Specifications

Source material has tested negative for HIV and HBsAg.

Physical form

Lyophilized powder containing sodium citrate and sodium chloride.

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

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Customers Also Viewed

J G White
The American journal of pathology, 137(4), 989-998 (1990-10-01)
Glycoprotein (GP)IIb-IIIa receptors on human platelets in suspension and after surface activation bind a variety of specific antibodies and ligands and transport them across the outside of the plasma membrane by processes of clustering, patching and capping, and endocytosis to
Mika Martiskainen et al.
BMC neurology, 14, 137-137 (2014-06-25)
Women die of stroke more often than men. After menopause, the incidence of ischemic stroke increases rapidly. Elevated fibrinogen levels and smoking have been associated with an increased risk of stroke. In gene-cluster haplotype analyses, the beta-fibrinogen (FGB) promoter -455
Ronen Ben-Ami et al.
American journal of physiology. Heart and circulatory physiology, 285(6), H2663-H2669 (2003-07-19)
Therapeutic administration of immunoglobulins (Ig) has the potential to precipitate thrombotic events. This phenomenon may be explained by red blood cell (RBC) aggregation, which can be potentiated by Ig. The contribution of plasma albumin and fibrinogen to Ig-induced RBC aggregation
Sung Jean Park et al.
International journal of nanomedicine, 7, 4325-4333 (2012-08-24)
The conformational changes of plasma protein structures in response to carbon nanotubes are critical for determining the nanotoxicity and blood coagulation effects of carbon nanotubes. In this study, we identified that the functional intensity of carboxyl groups on carbon nanotubes
R G Humphrey et al.
Placenta, 26(6), 491-497 (2005-06-14)
We hypothesized that fibrin enhances apoptosis and modulates differentiation of trophoblast in vitro. Cytotrophoblasts isolated from normal term human placentas were cultured < or =72 h in DMEM-10%-FBS on a fibrin matrix in standard or hypoxic conditions. Trophoblasts were cultured

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