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Merck
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Principaux documents

A9667

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

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

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About This Item

Numéro MDL:
MFCD00162430
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46
Le tarif et la disponibilité ne sont pas disponibles actuellement.

Source biologique

goat

Niveau de qualité

200

Conjugué

peroxidase conjugate

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Technique(s)

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Description générale

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.

Immunogène

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.

Forme physique

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

Notes préparatoires

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

Clause de non-responsabilité

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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Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H317,H334

Classification des risques

Resp. Sens. 1 - Skin Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
0000317614
0000310338
0000222583
0000237201
0000213707

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Consulter la Bibliothèque de documents

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)
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)
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
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
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
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