Sigma

Fibrinopeptide A human

F3254 -

≥96% (HPLC)

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Description

Amino Acid Sequence

Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg

Biochem/physiol Actions

Fibrin polymerization is initiated by thrombin cleavage of fibrinopeptide A from fibrinogen α chains, exposing two E domain E(A) sites. The phenylalanine at α chain residue 8 is important for efficient thrombin-catalyzed proteolysis of fibrinogen. Substitution of tyrosine for phenylalanine blocks sequential fibrinopeptide release and, thus, blocks polymerization and clot formation.

Price and Availability

Customers Also Viewed

50-70% protein (≥80% of protein is clottable)

≥97% (HPLC)


Documents

Certificate of Analysis

Certificate of Origin

Gene Information
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Safety Information

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Articles

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References

Johnson, B.J. and May, W.P. J. Pharm. Sci. 58, 1568, (1969) Abstract

Rooney, M.M., Mullin, J.L., Lord, S.T., Substitution of tyrosine for phenylalanine in fibrinopeptide A results in preferential thrombin cleavage of fibrinopeptide B from fibrinogen. Biochemistry 37, 13704-13709, (1998) Abstract

Mosesson, M.W., Fibrinogen and fibrin polymerization: appraisal of the binding events that accompany fibrin generation and fibrin clot assembly. Blood Coag. Fibrinolysis 8, 257-267, (1997)

Weitz, J.I., Elevated fibrinopeptide A and B levels during thrombolytic therapy: real or artefactual. Thromb. Haemost. 75, 529-535, (1996) Abstract

Baker, E.S., et al., Simultaneous fragmentation of multiple ions using IMS drift time dependent collision energies. J. Am. Soc. Mass Spectrom. 19, 411-9, (2008) Abstract


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