Fibrinogen beta chain Antibody #54390
Filter:
- WB
Supporting Data
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 55 |
SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Fibrinogen beta chain Antibody recognizes endogenous levels of total fibrinogen beta chain protein. This antibody does not cross-react with either fibrinogen Aα or fibrinogen γ proteins.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn190 of human fibrinogen beta chain protein. Antibodies are purified by peptide affinity chromatography.
Background
Fibrinogen is a large, multimeric plasma glycoprotein that is constitutively synthesized by liver hepatocytes. As a key component of blood clots, fibrinogen plays a central role in hemostasis and thrombosis. In total, six polypeptide chains (2Aα, 2Bβ, and 2γ) are produced intracellularly in a coordinated manner, which are then covalently linked together by a network of disulfide bonds to form a fibrinogen heterohexamer (1). Research studies have shown that expression of the three fibrinogen genes is upregulated as part of the acute phase inflammatory response (2,3).
Upon engagement of the clotting cascade, thrombin-mediated cleavage of the fibrinogen Aα and Bβ chains creates fibrin monomers and a platform for the polymerization of fibrin monomers into protofibrils and an insoluble web of stable fibrin fibers (4,5). Whereas thrombin is the enzyme that drives fibrin polymerization and clot formation, plasmin is the enzymatic counterpart that facilitates fibrinolysis and clot breakdown (6).
In addition to its position as a central node in the normal coagulation cascade, dysregulated fibrin deposition has been observed in pathological conditions such as cancer and viral infection (7,8).
Upon engagement of the clotting cascade, thrombin-mediated cleavage of the fibrinogen Aα and Bβ chains creates fibrin monomers and a platform for the polymerization of fibrin monomers into protofibrils and an insoluble web of stable fibrin fibers (4,5). Whereas thrombin is the enzyme that drives fibrin polymerization and clot formation, plasmin is the enzymatic counterpart that facilitates fibrinolysis and clot breakdown (6).
In addition to its position as a central node in the normal coagulation cascade, dysregulated fibrin deposition has been observed in pathological conditions such as cancer and viral infection (7,8).
- Chapin, J.C. and Hajjar, K.A. (2015) Blood Rev 29, 17-24.
- Dalmon, J. et al. (1993) Mol Cell Biol 13, 1183-93.
- Huber, P. et al. (1990) J Biol Chem 265, 5695-701.
- Lord, S.T. (2011) Arterioscler Thromb Vasc Biol 31, 494-9.
- Yang, Z. et al. (2000) Proc Natl Acad Sci U S A 97, 14156-61.
- Cesarman-Maus, G. and Hajjar, K.A. (2005) Br J Haematol 129, 307-21.
- Fernandez, P.M. et al. (2004) Semin Thromb Hemost 30, 31-44.
- Merad, M. and Martin, J.C. (2020) Nat Rev Immunol 20, 355-362.
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