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

IgG fraction of antiserum, buffered aqueous solution

MDL number:

Quality Level

biological source


antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies




buffered aqueous solution


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


peroxidase conjugate

shipped in

dry ice

storage temp.


Related Categories

General description

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.
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.


IgE purified from human myeloma serum


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).


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.


Health hazard

Signal Word


Hazard Statements


NONH for all modes of transport

WGK Germany


Certificate of Analysis

Certificate of Origin

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...
Alok Kumar Verma et al.
Toxicology letters, 210(1), 24-33 (2012-01-31)
Allergy to chickpea or Garbanzo bean (Cicer arietinum) has been reported in the Indian population. Little information is found regarding allergenic events involved in the chickpea allergy; therefore, chickpea allergenicity assessment was undertaken. In vivo and ex vivo studies were...
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...
Middleton's Allergy 2-Volume Set: Principles and Practice (2013)
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)
Antibody-based serology tests are useful in identifying subjects with an adaptive immune response to the SARS-CoV-2 virus. Anti-human immunoglobulin antibodies allow for quick and simple, yet reliable assays with easy readouts and can also be adapted for high-throughput screening.
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