G3637
Globulins Cohn fraction IV-4 human
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Allgemeine Beschreibung
Cohn fraction IV consists of α and β-globulins. It is a plasma by-product produced during γ-globulin synthesis.
Anwendung
Globulins Cohn fraction IV-4 human has been used in differential scanning calorimetry (DSC) to test the effect of low-dose ionizing radiation. It has also been used in the preparation of plasma protein solution for biophysical studies.
Globulins may in binding of 5-methoxypsoralen to blood fractions. It may used as positive control for Granulocyte immunofluorescence test (GIFT). It may also used to study the thermal denaturation of mixtures of human serum proteins.
Biochem./physiol. Wirkung
The Cohn fraction IV (α-globin enriched) mediates the inhibition of brain neurotransmitter receptors.
Sonstige Hinweise
Predominantly α- and β-globulins
Haftungsausschluss
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.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Effects of low-dose ionizing radiation on alpha, beta-globulins solutions studied by DSC
Michnik A, et al.
Journal of Thermal Analysis and Calorimetry, 111(3), 1845-1852 (2013)
A C Andorn et al.
Proceedings of the National Academy of Sciences of the United States of America, 83(12), 4572-4575 (1986-06-01)
Human serum proteins are found in significant density in the neuropil in brains of demented individuals. The functional significance of these abnormally distributed proteins has been unknown. We now report that alpha-globulin-enriched fractions of human serum decrease the specific binding
P Muret et al.
Skin pharmacology : the official journal of the Skin Pharmacology Society, 6(1), 45-51 (1993-01-01)
The binding of 5-methoxypsoralen (5-MOP) to human serum and blood fractions was studied by equilibrium dialysis associated to high-performance liquid chromatography. 5-MOP serum binding was 95% and kept constant in the range of therapeutic concentrations. Albumin was the main binding
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