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Merck

F3379

Sigma-Aldrich

Fibrinopeptide B human

≥97% (HPLC)

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About This Item

Empirische Formel (Hill-System):
C66H93N19O25
CAS-Nummer:
Molekulargewicht:
1552.56
MDL-Nummer:
UNSPSC-Code:
12352200
PubChem Substanz-ID:

Biologische Quelle

human

Assay

≥97% (HPLC)

Form

powder

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

SMILES String

CC(C)C(NC(=O)CNC(=O)C1CCC(=O)N1)C(=O)NC(CC(N)=O)C(=O)NC(CC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CCC(O)=O)C(=O)NC(CCC(O)=O)C(=O)NCC(=O)NC(Cc2ccccc2)C(=O)NC(Cc3ccccc3)C(=O)NC(CO)C(=O)NC(C)C(=O)NC(CCCNC(N)=N)C(O)=O

InChI

1S/C66H93N19O25/c1-31(2)53(85-49(91)29-73-55(99)35-16-19-47(89)75-35)64(108)83-42(26-46(68)88)61(105)82-43(27-52(96)97)62(106)81-41(25-45(67)87)60(104)78-37(18-21-51(94)95)57(101)77-36(17-20-50(92)93)56(100)72-28-48(90)76-39(23-33-11-6-4-7-12-33)58(102)80-40(24-34-13-8-5-9-14-34)59(103)84-44(30-86)63(107)74-32(3)54(98)79-38(65(109)110)15-10-22-71-66(69)70/h4-9,11-14,31-32,35-44,53,86H,10,15-30H2,1-3H3,(H2,67,87)(H2,68,88)(H,72,100)(H,73,99)(H,74,107)(H,75,89)(H,76,90)(H,77,101)(H,78,104)(H,79,98)(H,80,102)(H,81,106)(H,82,105)(H,83,108)(H,84,103)(H,85,91)(H,92,93)(H,94,95)(H,96,97)(H,109,110)(H4,69,70,71)

InChIKey

MYRIFIVQGRMHRF-UHFFFAOYSA-N

Angaben zum Gen

human ... FGB(2244)

Amino Acid Sequence

Glp-Gly-Val-Asn-Asp-Asn-Glu-Glu-Gly-Phe-Phe-Ser-Ala-Arg

Allgemeine Beschreibung

Fibrinopeptide B (FPB) is produced during the cleavage of fibrinogen, by thrombin, to fibrin monomer. It is cleaved off from the N-terminal of the fibrinogen β chain. This peptide is composed of 14 amino acids.

Biochem./physiol. Wirkung

Cleavage of fibrinopeptide B from fibrinogen Bβ chains exposes E domain polymerization sites, E(B), that interact with platelets, fibroblasts and endothelial cells.
Fibrin formation is an essential part in wound healing and inflammation. Fibrinopeptide B (FPB) can also cause chemotactic migration of neutrophils, without the simultaneous release of lysosome enzymes. It is produced during the coagulation of fibrinogen, which is essential for physiological homeostasis. It is involved in various disorders such as thrombosis and disseminated intravascular coagulation.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Heinz Nika et al.
Journal of biomolecular techniques : JBT, 24(1), 17-31 (2013-04-02)
A sample preparation method for protein C-terminal peptide isolation has been developed. In this strategy, protein carboxylate glycinamidation was preceded by carboxyamidomethylation and optional α- and ϵ-amine acetylation in a one-pot reaction, followed by tryptic digestion of the modified protein.
T M Odrljin et al.
Blood, 88(6), 2050-2061 (1996-09-15)
Thrombin (IIa)-cleavage of fibrinogen (FBG) to form polymerized fibrin promotes endothelial cell spreading, proliferation, and von Willebrand factor release, requiring the exposure of the beta 15-42 domain. Studies reported here indicate that IIa-cleavage of fibrinopeptide B enhances exposure of a
Michael L Merchant et al.
Kidney international, 79(5), 546-554 (2010-12-15)
Biomarkers that evaluate the response to erythropoietic-stimulating agents largely measure inflammation and iron availability. While these are important factors in modifying an individual's response to these agents, they do not address all aspects of a poor response. To clarify this
A Vindigni et al.
Biochemistry, 35(14), 4417-4426 (1996-04-09)
The release of fibrinopeptides A and B by the slow and fast forms of thrombin was studied over the temperature range from 5 to 45 degrees C and the salt concentration range from 100 to 800 mM. The sequential mechanism
Bi-Ying Wei et al.
Journal of chromatography. A, 1217(44), 6927-6931 (2010-09-21)
Liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) with selective reaction monitoring (SRM) is a selective and sensitive method for quantitation of peptides. SRM is achieved via MS/MS utilizing collision-induced dissociation (CID) while monitoring unique precursor-product ion transitions. Low-energy CID

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