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About This Item
Conjugate:
peroxidase conjugate
Clone:
polyclonal
Application:
DB, ELISA (d)
Technique(s):
direct ELISA: 1:2,000, dot blot: 1:10,000 (chemiluminescent)
Citations:
26
biological source
goat
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
Quality Level
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.
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.
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
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).
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signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
Ayca Kiykim et al.
International archives of allergy and immunology, 178(1), 1-9 (2018-11-08)
About 65-80% of children with IgE-mediated cow's milk allergy (CMA) can tolerate extensively heated milk. We have invested in the mass fabrication of a test product containing milk protein baked at 180°C for 30 min (SUTMEK-milk) and a milk-free placebo
Quantitative and qualitative optimization of allergen extraction from peanut and selected tree nuts. Part 2. Optimization of buffer and ionic strength using a full factorial experimental design
LHocine L, et al.
Food Chemistry, 194, 820-827 (2016)
Nataly Cancelliere et al.
Biomedical reports, 12(6), 326-332 (2020-04-30)
Parietaria judaica and P. officinalis are the two most common subspecies of the Parietaria genus. P. judaica and P. officinalis have exhibited cross-reactivity in previous studies. P. judaica pollen is the main cause of allergy in the Mediterranean area. It
Detection of serum and salivary IgE and IgG1 immunoglobulins specific for diagnosis of food allergy.
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
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