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A9667

Sigma-Aldrich

Anti-Human IgE (ε-chain specific)−Peroxidase antibody produced in goat

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Goat Anti-Human IgE (ε-chain specific)−HRP

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About This Item

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

biological source

goat

Quality Level

conjugate

peroxidase conjugate

antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

direct ELISA: 1:2,000
dot blot: 1:10,000 (chemiluminescent)

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

IgEs are glycoprotein antibodies that regulate immunological responses to allergies and infections. These immunoglobulins have been implicated in mediating Type I hypersensitivity reactions . Elevated IgE levels have been associated with hyper IgE syndrome and allergic asthma. Anti-Human IgE ε-chain specific-Peroxidase antibody binds to human IgE as against human IgG, and Bence Jones κ and λ myeloma proteins.
Immunoglobulin E (IgE) belongs to the immunoglobulin family and consists of epsilon(ε) heavy chain in the constant (C) region. IgE has a monomeric structure with an extra domain in the constant region.

Immunogen

IgE purified from human myeloma serum

Application

Anti-Human IgE (ε-chain specific)-Peroxidase antibody produced in goat has been used in IgE immunoblotting and in western blotting to analyse IgE binding efficiency.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 0.05% MIT

Preparation Note

Prepared by the two-step glutaraldehyde method described by Avrameas, S., et al., Scand. J. Immunol., 8, Suppl. 7, 7 (1978).

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.

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Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Amita Misra et al.
GM crops & food, 3(4), 273-282 (2012-06-30)
Genetically modified (GM) mustard line (V4) with increased carotenoid content was compared with native mustard to find the difference in allergenic potential, if any. Simulated gastric fluid (SGF) digestibility of crude protein extract from GM as well as its native
Marília Porto Oliveira Nunes et al.
PloS one, 14(4), e0214745-e0214745 (2019-04-18)
Given the growing incidence and prevalence of life-threatening food allergies, health concerns have raised new perspectives for in vivo and in vitro diagnostic methodologies, pointing to saliva as a promising material, already used to diagnose other pathologies. Based on the
Y Shahali et al.
Allergy, 64(12), 1773-1779 (2009-07-25)
The allergenic characteristics of pollen and their levels of expression may vary depending on the plant species, the degree of maturation and the influence of environmental factors such as climate and atmospheric pollution. The objective of this survey was the
Effects of different thermal processing methods on the structure and allergenicity of peanut allergen Ara h 1
Tian Y, et al.
Food Science & Nutrition, 6(6), 1706-1714 (2018)
Yang Tian et al.
Food science & nutrition, 6(6), 1706-1714 (2018-09-28)
Boiling and frying can alter the structure of peanut allergens and therefore change the IgE-binding capacity of the Ara h 1. In this research, we aim to clarify the connections between structural changes and the allergenicity alteration, and recommend an

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