Fibrin
目录号 : GC39150
Fibrin 是从牛血液中分离出来的一种不溶性蛋白质，可响应出血而产生。Fibrin 是血凝块的主要成分，可用于凝血。
Cas No.:9001-31-4
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Fibrin, isolated from bovine blood, is an insoluble protein produced in response to bleeding. Fibrin is the major component of the blood clot and is used for coagulation[1].
[1]. Paulson CN, et al. The anti-parasitic agent suramin and several of its analogues are inhibitors of the DNA bindingprotein Mcm10. Open Biol. 2019 Aug 30;9(8):190117.
| Purity | Source | bovine blood | |
| Phycical Appearance | A Solid | Shipping Condition | Store at -20°C |
| Solubility | H2O : < 0.1 mg/mL (ultrasonic) (insoluble); DMSO : < 1 mg/mL (ultrasonic) (insoluble or slightly soluble) | ||
| Biological Activity | Fibrin, isolated from bovine blood, is an insoluble protein produced in response to bleeding. Fibrin is the major component of the blood clot and is used for coagulation[1] | ||
Fibrin, isolated from bovine blood, is an insoluble protein produced in response to bleeding. Fibrin is the major component of the blood clot and is used for coagulation[1]
Fibrinogen and Fibrin
Adv Protein Chem 2005;70:247-99.PMID:15837518DOI:10.1016/S0065-3233(05)70008-5.
Fibrinogen is a large, complex, fibrous glycoprotein with three pairs of polypeptide chains linked together by 29 disulfide bonds. It is 45 nm in length, with globular domains at each end and in the middle connected by alpha-helical coiled-coil rods. Both strongly and weakly bound calcium ions are important for maintenance of fibrinogen's structure and functions. The fibrinopeptides, which are in the central region, are cleaved by thrombin to convert soluble fibrinogen to insoluble Fibrin polymer, via intermolecular interactions of the "knobs" exposed by fibrinopeptide removal with "holes" always exposed at the ends of the molecules. Fibrin monomers polymerize via these specific and tightly controlled binding interactions to make half-staggered oligomers that lengthen into protofibrils. The protofibrils aggregate laterally to make fibers, which then branch to yield a three-dimensional network-the Fibrin clot-essential for hemostasis. X-ray crystallographic structures of portions of fibrinogen have provided some details on how these interactions occur. Finally, the transglutaminase, Factor XIIIa, covalently binds specific glutamine residues in one Fibrin molecule to lysine residues in another via isopeptide bonds, stabilizing the clot against mechanical, chemical, and proteolytic insults. The gene regulation of fibrinogen synthesis and its assembly into multichain complexes proceed via a series of well-defined steps. Alternate splicing of two of the chains yields common variant molecular isoforms. The mechanical properties of clots, which can be quite variable, are essential to Fibrin's functions in hemostasis and wound healing. The fibrinolytic system, with the zymogen plasminogen binding to Fibrin together with tissue-type plasminogen activator to promote activation to the active enzyme plasmin, results in digestion of Fibrin at specific lysine residues. Fibrin(ogen) also specifically binds a variety of other proteins, including fibronectin, albumin, thrombospondin, von Willebrand factor, fibulin, fibroblast growth factor-2, vascular endothelial growth factor, and interleukin-1. Studies of naturally occurring dysfibrinogenemias and variant molecules have increased our understanding of fibrinogen's functions. Fibrinogen binds to activated alphaIIbbeta3 integrin on the platelet surface, forming bridges responsible for platelet aggregation in hemostasis, and also has important adhesive and inflammatory functions through specific interactions with other cells. Fibrinogen-like domains originated early in evolution, and it is likely that their specific and tightly controlled intermolecular interactions are involved in other aspects of cellular function and developmental biology.
Fibrin Formation, Structure and Properties
Subcell Biochem 2017;82:405-456.PMID:28101869DOI:10.1007/978-3-319-49674-0_13.
Fibrinogen and Fibrin are essential for hemostasis and are major factors in thrombosis, wound healing, and several other biological functions and pathological conditions. The X-ray crystallographic structure of major parts of Fibrin(ogen), together with computational reconstructions of missing portions and numerous biochemical and biophysical studies, have provided a wealth of data to interpret molecular mechanisms of Fibrin formation, its organization, and properties. On cleavage of fibrinopeptides by thrombin, fibrinogen is converted to Fibrin monomers, which interact via knobs exposed by fibrinopeptide removal in the central region, with holes always exposed at the ends of the molecules. The resulting half-staggered, double-stranded oligomers lengthen into protofibrils, which aggregate laterally to make fibers, which then branch to yield a three-dimensional network. Much is now known about the structural origins of clot mechanical properties, including changes in fiber orientation, stretching and buckling, and forced unfolding of molecular domains. Studies of congenital fibrinogen variants and post-translational modifications have increased our understanding of the structure and functions of Fibrin(ogen). The fibrinolytic system, with the zymogen plasminogen binding to Fibrin together with tissue-type plasminogen activator to promote activation to the active proteolytic enzyme, plasmin, results in digestion of Fibrin at specific lysine residues. In spite of a great increase in our knowledge of all these interconnected processes, much about the molecular mechanisms of the biological functions of Fibrin(ogen) remains unknown, including some basic aspects of clotting, fibrinolysis, and molecular origins of Fibrin mechanical properties. Even less is known concerning more complex (patho)physiological implications of fibrinogen and Fibrin.
Platelet-rich Fibrin (PRF): a second-generation platelet concentrate. Part I: technological concepts and evolution
Oral Surg Oral Med Oral Pathol Oral Radiol Endod 2006 Mar;101(3):e37-44.PMID:16504849DOI:10.1016/j.tripleo.2005.07.008.
Platelet-rich Fibrin (PRF) belongs to a new generation of platelet concentrates geared to simplified preparation without biochemical blood handling. In this initial article, we describe the conceptual and technical evolution from Fibrin glues to platelet concentrates. This retrospective analysis is necessary for the understanding of Fibrin technologies and the evaluation of the biochemical properties of 3 generations of surgical additives, respectively Fibrin adhesives, concentrated platelet-rich plasma (cPRP) and PRF. Indeed, the 3-dimensional Fibrin architecture is deeply dependent on artificial clinical polymerization processes, such as massive bovine thrombin addition. Currently, the slow polymerization during PRF preparation seems to generate a Fibrin network very similar to the natural one. Such a network leads to a more efficient cell migration and proliferation and thus cicatrization.
Fibrin mechanical properties and their structural origins
Matrix Biol 2017 Jul;60-61:110-123.PMID:27553509DOI:10.1016/j.matbio.2016.08.003.
Fibrin is a protein polymer that is essential for hemostasis and thrombosis, wound healing, and several other biological functions and pathological conditions that involve extracellular matrix. In addition to molecular and cellular interactions, Fibrin mechanics has been recently shown to underlie clot behavior in the highly dynamic intra- and extravascular environments. Fibrin has both elastic and viscous properties. Perhaps the most remarkable rheological feature of the Fibrin network is an extremely high elasticity and stability despite very low protein content. Another important mechanical property that is common to many filamentous protein polymers but not other polymers is stiffening occurring in response to shear, tension, or compression. New data has begun to provide a structural basis for the unique mechanical behavior of Fibrin that originates from its complex multi-scale hierarchical structure. The mechanical behavior of the whole Fibrin gel is governed largely by the properties of single fibers and their ensembles, including changes in fiber orientation, stretching, bending, and buckling. The properties of individual Fibrin fibers are determined by the number and packing arrangements of double-stranded half-staggered protofibrils, which still remain poorly understood. It has also been proposed that forced unfolding of sub-molecular structures, including elongation of flexible and relatively unstructured portions of Fibrin molecules, can contribute to Fibrin deformations. In spite of a great increase in our knowledge of the structural mechanics of Fibrin, much about the mechanisms of Fibrin's biological functions remains unknown. Fibrin deformability is not only an essential part of the biomechanics of hemostasis and thrombosis, but also a rapidly developing field of bioengineering that uses Fibrin as a versatile biomaterial with exceptional and tunable biochemical and mechanical properties.
Fibrin-based delivery strategies for acute and chronic wound healing
Adv Drug Deliv Rev 2018 Apr;129:134-147.PMID:29247766DOI:10.1016/j.addr.2017.12.007.
Fibrin, a natural hydrogel, is the end product of the physiological blood coagulation cascade and naturally involved in wound healing. Beyond its role in hemostasis, it acts as a local reservoir for growth factors and as a provisional matrix for invading cells that drive the regenerative process. Its unique intrinsic features do not only promote wound healing directly via modulation of cell behavior but it can also be fine-tuned to evolve into a delivery system for sustained release of therapeutic biomolecules, cells and gene vectors. To further augment tissue regeneration potential, current strategies exploit and modify the chemical and physical characteristics of Fibrin to employ combined incorporation of several factors and their timed release. In this work we show advanced therapeutic approaches employing Fibrin matrices in wound healing and cover the many possibilities Fibrin offers to the field of regenerative medicine.