F4639
Monoclonal Anti-Fibrinogen antibody produced in mouse
clone FG-21, ascites fluid
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About This Item
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biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
FG-21, monoclonal
contains
15 mM sodium azide
species reactivity
human, baboon
technique(s)
indirect ELISA: 1:4,000
isotype
IgG2a
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
Fibrinogen, is a thrombin-coagulable soluble plasma 340kDa glycoprotein, composed of paired sets of three subunits i.e. α, β, γ. Among three subunits, β and γ subunits contain one N-glycosylation site, which is occupied by a biantennary N-glycan. It contains three pairs of disulfide bonded chains called α, β, γ which further folded into four structural domains: the D, E, connector and the COOH-terminal region of the Aα chain.
Monoclonal Anti-Fibrinogen (mouse IgG2a isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.
Specificity
The antibody is specific for human fibrinogen and recognizes an epitope sensitive to reduction commonly used in immunoblotting assays. It also reacts with synthetic human fibrinopeptides A and B, fibrinogen related peptides and baboon fibrinogen. No cross-reactivity with bovine, pig, sheep, horse, dog, goat, rabbit, guinea pig, or rat is observed.
Immunogen
purified haptoglobin from pooled human plasma containing the three major haptotypes.
Application
Monoclonal Anti-Fibrinogen antibody produced in mouse has been used in:
- enzyme linked immunosorbent assay (ELISA)
- immunoblotting
- fibrinogen adsorption assay
Biochem/physiol Actions
Fibrinogen, a blood coagulation protein, is regarded as the central protein in the blood coagulation system.Fibrinogen plays a crucial role in protecting the vascular network against the loss of blood after tissue injury.
Plasmin attacks the Aα chain COOH domain to produce the heterogeneous fragment X. After a series of degradation, it ended with terminal digestion products: fragments D and E which represent the major globular domains in fibrinogen. Mutations in this gene leads to several disorders including hypofibrinogenemia, afibrinogenemia.
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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Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Photon-modulated changes of cell attachments on poly (spiropyran-co-methyl methacrylate) membranes
Higuchi A, et al.
Biomacromolecules, 5(5), 1770-1774 (2004)
Identification of Apo-A1 as a biomarker for early diagnosis of bladder transitional cell carcinoma
Li H, et al.
Proteome Science, 9(1), 21-21 (2011)
N E Kirschbaum et al.
The Journal of biological chemistry, 265(23), 13669-13676 (1990-08-15)
The COOH-terminal portion of the A alpha chain of human fibrinogen is highly susceptible to proteolytic degradation. This property has prevented isolation of the COOH-terminal domain of fibrinogen for the direct investigation of its functional characteristics. Human fibrinogen was degraded
Preservation of hematopoietic stem and progenitor cells from umbilical cord blood stored in a surface derivatized with polymer nanosegments
Higuchi A, et al.
Biomacromolecules, 9(2), 634-639 (2008)
Y Fang et al.
Haemophilia : the official journal of the World Federation of Hemophilia, 12(6), 615-620 (2006-11-07)
Congenital afibrinogenaemia is a rare autosomal recessive disorder, characterized by the complete absence or extremely reduced level of fibrinogen (Fg). We attempted to analyse the phenotype and genotype in two Chinese families with congenital afibrinogenaemia. Coagulation studies including activated partial
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