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Documenti fondamentali

G3637

Sigma-Aldrich

Globulins Cohn fraction IV-4 human

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About This Item

Numero CAS:
Numero CE:
Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.61

Origine biologica

human

Livello qualitativo

Stato

powder

Solubilità

H2O: soluble 50 mg/mL

Temperatura di conservazione

2-8°C

Descrizione generale

Cohn fraction IV consists of α and β-globulins. It is a plasma by-product produced during γ-globulin synthesis.

Applicazioni

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.

Azioni biochim/fisiol

The Cohn fraction IV (α-globin enriched) mediates the inhibition of brain neurotransmitter receptors.

Altre note

Predominantly α- and β-globulins

Esclusione di responsabilità

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.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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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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