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F3379

Sigma-Aldrich

Fibrinopeptide B human

≥97% (HPLC)

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About This Item

Formule empirique (notation de Hill):
C66H93N19O25
Numéro CAS:
36204-23-6
Poids moléculaire :
1552.56
Numéro MDL:
MFCD00076439
Code UNSPSC :
12352200
ID de substance PubChem :
24894841

Source biologique

human

Pureté

≥97% (HPLC)

Forme

powder

Numéro d'accès UniProt

P02675

Température de stockage

−20°C

Chaîne SMILES 

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)

Clé InChI

MYRIFIVQGRMHRF-UHFFFAOYSA-N

Informations sur le gène

human ... FGB(2244)

Amino Acid Sequence

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

Description générale

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.

Actions biochimiques/physiologiques

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.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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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
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
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.
Ernst Pittenauer et al.
Journal of proteomics, 74(7), 975-981 (2010-10-26)
The desorption/ionization behavior of individual peptides, an equimolare peptide mixture and a tryptic digest was investigated by AP-MALDI-IT-MS using four different target materials (gold-covered stainless steel (SS), titanium nitride-covered SS, hand-polished SS, and microdiamond-covered hardmetal) under identical conditions. Gold-covered as
Xiaohua Liu et al.
Journal of the American Society for Mass Spectrometry, 22(12), 2125-2136 (2011-10-15)
A new model has been developed to account for adduct formation on multiply charged peptides observed in negative ion electrospray mass spectrometry. To obtain a stable adduct, the model necessitates an approximate matching of apparent gas-phase basicity (GB(app)) of a
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