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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

Key Documents

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Product Name

Anti-Human IgE (ε-chain specific)−Peroxidase antibody produced in goat, IgG fraction of antiserum, buffered aqueous solution

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

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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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

常规特殊物品
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Certificates of Analysis (COA)

Lot/Batch Number
0000317614
0000310338
0000317614
0000310338
0000237201

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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
Immunoglobulin E reactivity to Arizona cypress pollen extracts: evidence for a 35-kDa allergen.
Y Shahali et al.
Allergy, 64(11), 1687-1688 (2009-10-03)
Wei-Wei Ni et al.
Molecular medicine reports, 16(3), 2851-2855 (2017-06-29)
Platanus acerifolia (P. acerifolia) is an important cause of pollinosis in cities. The use of allergen extracts on patients with allergic diseases is the most commonly applied method to attempt to treat pollinosis. Pla a 3, a non‑specific lipid transfer protein
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