9001-32-5 Usage
Description
HUMAN FIBRINOGEN is a soluble plasma glycoprotein produced by the liver, which plays a crucial role in the blood coagulation process. It is converted by thrombin into fibrin, helping in blood clot formation. As a natural blood protein, it serves as an alternative to traditional sources of fibrinogen such as blood products, fresh frozen plasma, and cryoprecipitate.
Uses
Used in Blood Coagulation:
HUMAN FIBRINOGEN is used as a blood coagulation agent for promoting blood clot formation. It is particularly useful in situations where traditional sources of fibrinogen, such as blood products, fresh frozen plasma, and cryoprecipitate, are not readily available or suitable.
Used in Diagnostic Aids:
HUMAN FIBRINOGEN serves as a diagnostic aid in vascular patency, helping to assess the integrity and function of blood vessels.
Used as a Radioactive Agent:
In medical imaging and diagnostics, HUMAN FIBRINOGEN can be used as a radioactive agent to enhance the visibility of blood vessels and other structures during imaging procedures.
Used in Growth Factor Solutions Preparation:
HUMAN FIBRINOGEN has been used in the preparation of growth factor solutions, which are essential for various biological and medical applications, including tissue repair and regeneration.
Used in Immunoblot Analysis:
HUMAN FIBRINOGEN can be applied on discontinuous SDS-polyacrylamide gels for the detection of IgG (immunoglobulins) type antibodies by immunoblot analysis, aiding in the study of immune responses and antibody production.
Used in Cell Transplantation:
HUMAN FIBRINOGEN can be mixed with cell suspensions to form a clot, which helps retain the cells and prevent their dispersion during transplantation. This application is particularly useful in tissue engineering and regenerative medicine, where maintaining cell integrity and viability is crucial for successful transplantation outcomes.
Biochem/physiol Actions
Fibrinogen is an acute phase protein that is part of the coagulation cascade of proteins. The end result of the cascade is the production of thrombin that converts fibrinogen to fibrin. Thrombin rapidly proteolyses fibrinogen, releasing fibrinopeptide A. The loss of this small peptide is not sufficient to make the resulting fibrin molecule insoluble, but it tends to form complexes with adjacent fibrin and fibrinogen molecules. Thrombin then cleaves a second peptide, fibrinopeptide B, from fibrin and the fibrin monomers formed then polymerize spontaneously to form an insoluble gel. The polymerized fibrin is held together by noncovalent and electrostatic forces and stabilized by the transamidating enzyme, factor XIIIa, that is produced by the action of thrombin on factor XIII. The insoluble fibrin aggregates (clots) and aggregated platelets then block the damaged blood vessel and prevent further bleeding. The amount of fibrinogen in the plasma can serve as a nonspecific indicator of whether or not an inflammatory process is present in the body. Fibrinogen from any mammalian source will be cleaved by thrombin from any mammalian source.
Purification Methods
A likely impurity is plasminogen. It is purified by glycine precipitation [Mosesson & Sherry Biochemistry 5 2829 1966] to obtain fractions 1-2, then further purified [Blomb.ck & Blomb.ck Arkiv Kemi 10 415 1956] and contaminating plasminogen is removed by passage through a lysine-Sepharose column. Such preparations are at least 95% clottable as determined by Mosesson and Sherry's method (above ref.) in which the OD280 is measured before and after clotting with 5 Units/mL of thrombin (> 3000U/mg). All fibrinogen preparations are treated with calf intestinal alkaline phosphatase to convert any fibrinogen peptide-AP to fibrinogen peptide-A by removing serine-bound phosphate. Solutions are then lyophilised and stored at -20o. [Higgins & Shafer J Biol Chem 256 12013 1981.] It is sparingly soluble in H2O. Aqueous solutions are viscous with isoelectric point at pH 5.5. It is readily denatured by heating above 56o or by chemical agents, e.g. salicylaldehyde, naphthoquinone sulfonates, ninhydrin or alloxan. [Edsall et al. J Am Chem Soc 69 2731 1947, Purification: Cama et al. Naturwissenschaften 48 574 1961, Lorand & Middlebrook Science 118 515 1953, cf. Fuller in Methods Enzymol 163 474 1988.] For plasminogen-deficient fibrinogen from blood plasma, the anticoagulated blood is centrifuged and the plasma is frozen and washed with saline solution. It is treated with charcoal, freeze-thawed and dialysed versus Tris/NaCl buffer. [Maxwell & Nikel Biochemical Preparations 12 16 1968.]
Check Digit Verification of cas no
The CAS Registry Mumber 9001-32-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 9,0,0 and 1 respectively; the second part has 2 digits, 3 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 9001-32:
(6*9)+(5*0)+(4*0)+(3*1)+(2*3)+(1*2)=65
65 % 10 = 5
So 9001-32-5 is a valid CAS Registry Number.
