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
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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
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.
Not finding the right product?
Try our Product Selector Tool.
related product
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
W S Lexmond et al.
Allergy, 72(12), 1916-1924 (2017-06-11)
Food allergies are a growing health problem, and the development of therapies that prevent disease onset is limited by the lack of adjuvant-free experimental animal models. We compared allergic sensitization in patients with food allergy or Wiskott-Aldrich syndrome (WAS) and
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
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
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
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)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service