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F9902

Sigma-Aldrich

Monoclonal Anti-Fibrinogen antibody produced in mouse

clone 85D4, ascites fluid

Synonym(s):

Anti-Fib2

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

85D4, monoclonal

contains

15 mM sodium azide

species reactivity

pig, sheep, rabbit, bovine, baboon, human, goat, canine

technique(s)

dot blot: suitable
indirect ELISA: 1:8,000
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Fibrinogen is a blood coagulation protein that consists of Aα, Bβ and γ polypeptide chains. Fibrinogen expression is induced by acute-inflammatory responses and has also been associated with the risk of cardiovascular disorders. Monoclonal Anti-Fibrinogen antibody recognizes a conformational epitope, which is destroyed by the cleavage of the γ (302-303) bond. This epitope is found in fibrinogen and in fibrin monomers (devoid of either fibrinopeptide A, or both A and B fibrinopeptides), when they are immobilized on ELISA plates. The antibody reacts with the D-dimer and D-fragment. It does not recognize individual fibrinogen/fibrin chains in denatured-reduced forms or their proteolytic fragments. The E fragment is not recognized by the antibody. The antibody reacts with greater avidity with protofibrils than with wider fibrin fibers in electron microscopic analysis. Monoclonal Anti-Fibrinogen is specific for fibrinogen and fibrin in humans, baboons, bovines, sheep, goats, pigs, rabbits and dogs.
Fibrinogen was the first blood coagulation factor to be identified, and it is a precursor of fibrin protein. The three polypeptide chains are coded by three genes located on human chromosome 4q23-q32, and spans 51kb.

Specificity

The product recognizes a conformational epitope, which is destroyed by the cleavage of the γ (302-303) bond. This epitope is found in both fibrinogen and in fibrin monomers, devoid of either fibrinopeptide A, or both A and B fibrinopeptides, when they are immobilized on ELISA plates. The antibody reacts with the D-dimer and D-fragment. It does not recognize individual fibrinogen/fibrin chains in the denatured-reduced form and their proteolytic fragments. The E fragment is not recognized by the antibody. Using electron microscopy, the antibody reacts with greater avidity with protofibrils than with wider fibrin fibers.

Immunogen

human fibrin degradation products

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Monoclonal Anti-Fibrinogen antibody is suitable for use in indirect ELISA, dot blot (1:1000 using human fibrinogen), and western blot.
Monoclonal Anti-Fibrinogen antibody produced in mouse has been used in immunohistochemistry and confocal laser scanning microscopy.

Biochem/physiol Actions

Fibrinogen is an acute-phase inflammatory protein, which plays an essential role in blood clotting.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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Plasma fibrinogen lever and risk of coronary heart disease among Chinese population: a systematic review and meta-analysis
Song B, et al.
International Journal of Clinical and Experimental Medicine, 8(8), 95-95 (2015)
Martin T Matter et al.
ACS applied materials & interfaces, 13(28), 33300-33310 (2021-07-14)
Dental implant failure remains a prevalent problem around the globe. The integration of implants at the interface of soft and hard tissues is complex and susceptible to instability and infections. Modifications to the surface of titanium implants have been developed
Katharina Gegenschatz-Schmid et al.
Acta biomaterialia, 137, 331-345 (2021-10-22)
Blood-contacting medical implants made of Nitinol and other titanium alloys, such as neurovascular flow diverters and peripheral stents, have the disadvantage of being highly thrombogenic. This makes the use of systemic (dual) anti-platelet/anticoagulant therapies inevitable with related risks of device
Vincent Milleret et al.
Clinical implant dentistry and related research, 21 Suppl 1, 8-14 (2019-03-01)
Dental implants often have surface modifications that alter surface topography and chemistry to improve osseointegration and thereby increase treatment predictability. Surface contact-induced blood coagulation is associated with the onset of osseointegration. To quantitatively evaluate the thrombogenicity of two commercially available
Melanie A Burkhardt et al.
Scientific reports, 6, 21071-21071 (2016-02-18)
Low correlations of cell culture data with clinical outcomes pose major medical challenges with costly consequences. While the majority of biomaterials are tested using in vitro cell monocultures, the importance of synergistic interactions between different cell types on paracrine signalling

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