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I4506

Sigma-Aldrich

IgG from human serum

reagent grade, ≥95% (SDS-PAGE), essentially salt-free, lyophilized powder

Synonym(s):

Human IgG

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About This Item

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

conjugate

unconjugated

Quality Level

grade

reagent grade

assay

≥95% (SDS-PAGE)

form

essentially salt-free, lyophilized powder

composition

Protein, ≥90%

technique(s)

ELISA: suitable
dot immunobinding: suitable
immunoelectrophoresis: suitable
western blot: suitable

Storage temp.

2-8°C

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General description

Purified Human IgG is isolated from pooled normal human serum by fractionation and ion-exchange chromatography. The product is supplied as an essentially salt-free (less than 1% sodium), lyophilized powder.

Application

IgG from human serum was used as a standard at a concentration of 1.274 mg/ml in ELISA to determine antibody responses to Porphyromonas gingivalis and Prevotella intermedia. It was used for immunolabeling of Vero, BHK and PtK2 cells at a concentration of 0.2 mg/ml. IgG from human serum was used as a standard in SDS-PAGE of anti-Shigella LPS antibodies.

Biochem/physiol Actions

IgG antibody subtype is the most abundant of 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 defense of the neonate against infections.

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.

related product

Product No.
Description
Pricing

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Nils A Brechmann et al.
Biotechnology progress, 35(3), e2775-e2775 (2019-01-11)
High capacity magnetic protein A agarose beads, LOABeads PrtA, were used in the development of a new process for affinity purification of monoclonal antibodies (mAbs) from non-clarified CHO cell broth using a pilot-scale magnetic separator. The LOABeads had a maximum
Youhei Egami et al.
Journal of cell science, 130(24), 4168-4179 (2017-11-09)
Phagosome formation is a complicated process that requires spatiotemporally regulated actin reorganization. We found that RhoC GTPase is a critical regulator of FcγR-mediated phagocytosis in macrophages. Our live-cell imaging revealed that RhoC, but not RhoA, is recruited to phagocytic cups
Katinka Döhner et al.
Molecular biology of the cell, 13(8), 2795-2809 (2002-08-16)
After fusion of the viral envelope with the plasma membrane, herpes simplex virus type 1 (HSV1) capsids are transported along microtubules (MTs) from the cell periphery to the nucleus. The motor ATPase cytoplasmic dynein and its multisubunit cofactor dynactin mediate
Egil S Blix et al.
Biology of blood and marrow transplantation : journal of the American Society for Blood and Marrow Transplantation, 21(5), 840-847 (2015-02-18)
Multiple myeloma (MM) is considered an incurable B cell malignancy, although many patients can benefit from high-dose therapy with autologous stem cell transplantation (ASCT) as a first-line treatment. In non-Hodgkin lymphoma (NHL), ASCT is usually performed after relapse with curative
Christopher Ashwood et al.
Journal of the American Society for Mass Spectrometry, 29(6), 1194-1209 (2018-04-01)
Profiling cellular protein glycosylation is challenging due to the presence of highly similar glycan structures that play diverse roles in cellular physiology. As the anomericity and the exact linkage type of a single glycosidic bond can influence glycan function, there

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