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Merck
CN

F5386

Fibrin from human plasma

insoluble powder

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.61
EC Number:
232-597-0
MDL number:
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Product Name

Fibrin from human plasma, insoluble powder

SMILES string

N(CC(=O)NC)C(=O)CN

InChI key

BWGVNKXGVNDBDI-UHFFFAOYSA-N

InChI

1S/C5H11N3O2/c1-7-5(10)3-8-4(9)2-6/h2-3,6H2,1H3,(H,7,10)(H,8,9)

biological source

human plasma

form

powder

technique(s)

indirect ELISA: suitable

UniProt accession no.

Quality Level

Gene Information

Application

Fibrin from human plasma has been used:
  • for in vitro cleavage of fibrinogen and fibrin
  • as a reference for true component analysis (TCA) and principal component analysis (PCA) of Raman spectra
  • as a reference in Raman spectroscopy to study the binding mechanisms and the binding efficiency of the different polyoxometalates (POMs)

Biochem/physiol Actions

Fibrin acts as an important bio-polymer in the primary blood clotting process. It creates a scaffold for infiltrating cells during tissue repair. Fibrin is widely used as a tissue sealant for tissue regeneration applications as it enables the formation of a biocompatible physical structure. It is also used in delivery systems for cells and bioactive molecules. The fibrin matrix resembles the native pancreas and can serve as a scaffold material for islet transplantation. Fibrin has been used in studies to obtain fibrin-specific monoclonal antibodies (mAbs). These mAbs may be used to determine their role in fibrin polymerization and use in fibrin quantification in blood plasma.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

General description

Fibrin is produced from cross-linking of fibrinogen by thrombin. Fibrinogen is made up of two monomers each containing three polypeptide chains. Fibrinogen is a major plasma protein.

Preparation Note

Prepared by clotting fibrinogen to yield a crosslinked fibrin

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

常规特殊物品
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Abraham R Alfonso et al.
Acta biomaterialia, 9(9), 8149-8157 (2013-06-26)
Tissue engineered heart valves (TEHVs) may provide a permanent solution to congenital heart valve disease by permitting somatic valve growth in the pediatric patient. However, to date, TEHV studies have focused primarily on collagen, the dominant component of valve extracellular
James C Fredenburgh et al.
The Journal of biological chemistry, 288(41), 29394-29402 (2013-08-31)
The nonspecific binding of heparin to plasma proteins compromises its anticoagulant activity by reducing the amount of heparin available to bind antithrombin. In addition, interaction of heparin with fibrin promotes formation of a ternary heparin-thrombin-fibrin complex that protects fibrin-bound thrombin
Kristen T Morin et al.
Experimental cell research, 319(16), 2409-2417 (2013-06-27)
In vitro models of endothelial assembly into microvessels are useful for the study of angiogenesis and vasculogenesis. In addition, such models may be used to provide the microvasculature required to sustain engineered tissues. A large range of in vitro models
The effect of etanercept on lung leukocyte margination and fibrin deposition after cardiac surgery.
Barry Dixon et al.
American journal of respiratory and critical care medicine, 188(6), 751-754 (2013-09-17)
Suk Ho Bhang et al.
Biomaterials, 34(30), 7247-7256 (2013-07-06)
While subcutaneous tissue has been proposed as a potential site for pancreatic islet transplantation, concern remains that the microvasculature of subcutaneous tissue is too poor to support transplanted islets. In an effort to overcome this limitation, we evaluated whether fibrin

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