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56834

Sigma-Aldrich

Immunoglobulin G from human serum

≥95% (GE)

Synonyme(s) :

Human IgG

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About This Item

Numéro MDL:
MFCD00163923
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Niveau de qualité

100

Pureté

≥95% (GE)

Forme

fibers

Technique(s)

radioimmunoassay: suitable

Impuretés

≤1.0% sodium
≤15% water

Solubilité

0.1 M NaCl: 10 mg/mL, clear to slightly turbid, colorless

Température de stockage

2-8°C

Description générale

Immunoglobulin G (IgG) subtype is the most abundant serum immunoglobulins of the immune system. It is secreted by B cells and is found in blood and extracellular fluids. IgG provides protection from infections caused by bacteria, fungi and viruses. Maternal IgG is transferred to fetus through the placenta that is vital for immune defence of the neonate against infections
Human IgG is purified from normal human serum and contains =1.0% sodium and =15% water.

Application

Immunoglobulin G from human serum may be used as a standard in solid-phase RIA, and to ensure precipitation in RIA for acetylcholine receptor and anti-acetylcholine receptor antibody. It may be used in preparation of soluble antigen containing tyrosine residues for iodination.

Autres remarques

Review

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Laura R Stingaciu et al.
Scientific reports, 6, 22148-22148 (2016-03-30)
A flexible linker region between three fragments allows antibodies to adjust their binding sites to an antigen or receptor. Using Neutron Spin Echo Spectroscopy we observed fragment motion on a timescale of 7 ns with motional amplitudes of about 1
Kang R Cho et al.
Journal of the American Chemical Society, 133(22), 8586-8593 (2011-05-04)
Aberrant protein aggregation causes numerous neurological diseases including Creutzfeldt-Jakob disease (CJD), but the aggregation mechanisms remain poorly understood. Here, we report AFM results on the formation pathways of β-oligomers and nonfibrillar aggregates from wild-type full-length recombinant human prion protein (WT)
Use of solid-phase radioimmunoassay specific for human IgG or human C3b to detect Fc gamma or C3b receptors on human lymphoblastoid cell surfaces.
R Frade et al.
Methods in enzymology, 93, 155-163 (1983-01-01)
Suicide of lymphoid cells.
A Basten et al.
Methods in enzymology, 108, 254-261 (1984-01-01)
V Cabiaux et al.
Biophysical journal, 73(1), 406-417 (1997-07-01)
Aquaporins are integral membrane proteins found in diverse animal and plant tissues that mediate the permeability of plasma membranes to water molecules. Projection maps of two-dimensional crystals of aquaporin-1 (AQP1) reconstituted in lipid membranes suggested the presence of six to
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Protocoles

HPLC Analysis of Immunoglobulin G (IgG) on Zenix® SEC-150 versus Zenix® SEC-300, Effect of Pore Size on Resolution

HPLC Analysis of Immunoglobulin G (IgG) on Zenix® SEC-150 versus Zenix® SEC-300, Effect of Pore Size on Resolution

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