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Merck
CN

A9667

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

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
MFCD00162430
Conjugate:
peroxidase conjugate
Clone:
polyclonal
Application:
DB, ELISA (d)
Citations:
26

Key Documents

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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

200

Related Categories

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
GHS08

signalword

Danger

hcodes

H317,H334

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

Regulatory Information

低风险生物材料
常规特殊物品
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Certificates of Analysis (COA)

Lot/Batch Number
0000533015
0000454854
0000454854
0000533015
0000317614

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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)
De-Wang Wang et al.
Molecular medicine reports, 17(1), 394-399 (2017-11-09)
Platanus acerifolia is one of the major sources of outdoor allergens to humans, and can induce allergic asthma, rhinitis, dermatitis and other allergic diseases. Pla a 2 is a polygalacturonase and represents the major allergen identified in P. acerifolia pollen. The aim
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
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
View All Related Papers

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