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I8640

Sigma-Aldrich

IgG from human serum

technical grade, ≥80% (SDS-PAGE), buffered aqueous solution

Synonym(s):

Human IgG

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

conjugate

unconjugated

Quality Level

grade

technical grade

assay

≥80% (SDS-PAGE)

form

buffered aqueous solution

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Human IgG antibodies are primarily responsible for the facilitation of humoral immune responses such as complement fixation, placental transport, and phagocytosis among many others. IgG from human serum can be used as an economical alternative for reagent grade immunoglobulins where high purity is not essential. It can also be used in immunoelectrophoresis. The product is reactive in humans.
IgG antibody 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 and 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 by fractionation.

Application

Purified human IgG may be used as a reference antigen, standard, blocking agent, or coating protein in a variety of immunoassays including ELISA, dot immunobinding, Western immunoblotting, immunodiffusion, and immunoelectrophoresis. Other applications include starting materials for the preparation of immunogens and solid phase immunoadsorbents. Technical grade human IgG may be used as an economical alternative to the reagent grade immunoglobulins, in applications where high purity is not required. IgG from human serum was used as ELISA standard in various studies. A concentration range of 200 μg/ml to 1 mg/ml of human IgG was used for blocking in flow cytometry.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.2, containing 15 mM sodium azide

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.

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Simone F A Wouters et al.
Bioconjugate chemistry, 31(3), 656-662 (2020-01-08)
Bioluminescent antibodies represent attractive detection agents in both bioanalytical assays and imaging. Currently, their preparation relies on genetic fusion of luciferases to antibodies or nonspecific chemical conjugation strategies. Here, we report a generic method to generate well-defined covalent antibody-luciferase conjugates
Gerlândia Neres Pontes et al.
FEMS immunology and medical microbiology, 47(3), 405-413 (2006-07-29)
We evaluated the ability of human maternal and cord serum antibodies to protect mice challenged with live Escherichia coli serotype O6:K2ac (E. coli O6). Mice received paired maternal or cord serum pools before a challenge with E. coli O6 to
Ruben Godoy-Silva et al.
Biotechnology and bioengineering, 102(4), 1119-1130 (2008-10-30)
The effect of hydrodynamic forces on animal cell cultures, while extensively studied, still lacks significant, fundamental understanding. A previous manuscript reported on the acute exposure of CHO cells to hydrodynamic forces in a second generation convergent-divergent microfluidic device (Mollet et
Silvia C W Ling et al.
Haematologica, 97(1), 64-72 (2011-10-14)
Multiple myeloma, a malignancy of the antibody-secreting plasma cells, remains incurable by current therapy. However, the proteasome inhibitor bortezomib and other new drugs are revolutionizing its treatment. It remains unclear why myelomas are peculiarly sensitive to bortezomib, or what causes
K M Dziegielewska et al.
The Histochemical journal, 33(8), 443-451 (2002-04-05)
Fetuin, a foetal protein of unknown function, has been shown to be expressed in both the immune and nervous systems, especially during development. Here, we show for the first time, that fetuin is abundantly present in many cells of the

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