56834
Immunoglobulin G from human serum
≥95% (GE)
Sinónimos:
Human IgG
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25 MG
MXP 4,624.00
100 MG
MXP 13,244.00
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25 MG
MXP 4,624.00
100 MG
MXP 13,244.00
About This Item
Productos recomendados
Quality Level
assay
≥95% (GE)
form
fibers
technique(s)
radioimmunoassay: suitable
impurities
≤1.0% sodium
≤15% water
solubility
0.1 M NaCl: 10 mg/mL, clear to slightly turbid, colorless
storage temp.
2-8°C
General description
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[1]
Human IgG is purified from normal human serum and contains =1.0% sodium and =15% water.
Human IgG is purified from normal human serum and contains =1.0% sodium and =15% water.
Application
Other Notes
Review[5]
Disclaimer
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.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Suicide of lymphoid cells.
A Basten et al.
Methods in enzymology, 108, 254-261 (1984-01-01)
Immunoglobulin G (IgG).
P D Gorevic et al.
Methods in enzymology, 116, 3-25 (1985-01-01)
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)
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
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)
Protocolos
HPLC Analysis of Immunoglobulin G (IgG) on Zenix® SEC-150 versus Zenix® SEC-300, Effect of Pore Size on Resolution
Active Filters
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