G3637
Globulins Cohn fraction IV-4 human
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About This Item
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General description
Cohn fraction IV consists of α and β-globulins. It is a plasma by-product produced during γ-globulin synthesis.
Application
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 Actions
The Cohn fraction IV (α-globin enriched) mediates the inhibition of brain neurotransmitter receptors.
Other Notes
Predominantly α- and β-globulins
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.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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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
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Effects of low-dose ionizing radiation on alpha, beta-globulins solutions studied by DSC
Journal of Thermal Analysis and Calorimetry, 111(3), 1845-1852 (2013)
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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