Key features and details
- Sensitivity: 0.4 µg/ml
- Range: 1.5 µg/ml - 15 µg/ml
- Sample type: Plasma
- Detection method: Colorimetric
- Assay type: Competitive
- Reacts with: Human
Product nameHuman Fibrinogen ELISA Kit
See all Fibrinogen kits
Intra-assay Sample n Mean SD CV% Overall 5.4% Inter-assay Sample n Mean SD CV% Overall 10.1%
Sensitivity= 0.4 µg/ml
Range1.5 µg/ml - 15 µg/ml
Assay time3h 00m
Assay durationMultiple steps standard assay
Species reactivityReacts with: Human
Human Fibrinogen in vitro competitive ELISA (Enzyme-Linked Immunosorbent Assay) kit is designed for the quantitative measurement of Fibrinogen levels in plasma.
A Fibrinogen specific antibody has been precoated onto 96-well plates and blocked. Standards or test samples are added to the wells and subsequently biotinylated Fibrinogen is added and then followed by washing with wash buffer. Streptavidin-Peroxidase Complex is added and unbound conjugates are washed away with wash buffer. TMB is then used to visualize Streptavidin-Peroxidase enzymatic reaction. TMB is catalyzed by Streptavidin-Peroxidase to produce a blue color product that changes into yellow after adding acidic stop solution. The density of yellow coloration is inversely proportional to the amount of Fibrinogen captured in plate.
Get better reproducibility in only 90 minutes with Human Fibrinogen ELISA Kit (ab208036) from our SimpleStep ELISA® range.
The entire kit may be stored at -20°C for long term storage before reconstitution - Avoid repeated freeze-thaw cycles.
Storage instructionsStore at -20°C. Please refer to protocols.
Components 1 x 96 tests 100X Streptavidin-Peroxidase Conjugate 1 x 80µl 10X Diluent N Concentrate 1 x 30ml 2X Biotinylated Human Fibrinogen (Lyophilized) 1 vial 20X Wash Buffer Concentrate 1 x 30ml Chromogen Substrate 1 x 8ml Fibrinogen Microplate (12 x 8 well strips) 1 unit Fibrinogen Standard 2 vials Sealing Tapes 3 units Stop Solution 1 x 12ml
FunctionFibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Involvement in diseaseDefects in FGA are a cause of congenital afibrinogenemia (CAFBN) [MIM:202400]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
Defects in FGA are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.
Sequence similaritiesContains 1 fibrinogen C-terminal domain.
DomainA long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
modificationsThe alpha chain is not glycosylated.
Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.
Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Phosphorylation sites are present in the extracellular medium.
- Information by UniProt
ab108842 has been referenced in 4 publications.
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