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A9792

Sigma-Aldrich

Anti-Chicken IgY (IgG) (whole molecule)−Peroxidase antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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Synonym(s):
Rabbit Anti-Chicken IgY (IgG) (whole molecule)−HRP
MDL number:
MFCD00162225
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

200

conjugate

peroxidase conjugate

antibody form

IgG fraction of antiserum

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

chicken

technique(s)

direct ELISA: 1:30,000
dot blot: 1:160,000 using indirect chemiluminescence system using 5 ng human IgG/dot and chicken anti-human IgG as the primary antibody and Luminol plus enhancer as the substrate.
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:500 using using human pancreas sections and chicken anti-human insulin as the primary antibody.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

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General description

Chicken IgY is made of two heavy (H) and two light (L) chains. Its molecular weight is about ~180 kDa.

Specificity

Rabbit Anti-Chicken IgY (IgG) (whole molecule)-Peroxidase antibody binds to chicken IgY.

Immunogen

purified chicken IgY (IgG)

Application

Anti-Chicken IgY (IgG) (whole molecule) FITC antibody has been used in immunohistology.
Avian proteins over expressed and purified from E. coli were analyzed by western blot using HRP-conjugated rabbit anti-chicken IgY as the secondary at 1:2000 dilution.
Rabbit Anti-Chicken IgY (IgG) (whole molecule)-Peroxidase antibody has been used for ELISA. The antibody can also be used for dot blot (1:160,000) and IHC (1:500) assays.

Biochem/physiol Actions

Chicken IgY is the major antibody found in chicken serum. Chickens generate a comparatively enhanced antibody response to mammalian antigenic proteins. These immunoglobulins do not bind to Fc receptors present in mammals and bacteria, and also do not interact with rheumatoid factors. Thus anti-chicken antibodies are useful analytical tools for various research applications.
IgY plays a major role in defense mechanism against systemic infections. It also possesses the ability to initiate anaphylactic reactions.

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.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H317,H334

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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G Haqshenas et al.
The Journal of general virology, 83(Pt 9), 2201-2209 (2002-08-20)
We recently identified a novel virus, designated avian hepatitis E virus (avian HEV), from chickens with hepatitis-splenomegaly (HS) syndrome in the USA. We showed that avian HEV is genetically related to swine and human HEVs. Here we report the antigenic
Energetic stress, immunosuppression and the costs of an antibody response.
Svensson, E., et al.
Functional Ecology, 12(6), 912-919 (1998)
N Obermüller et al.
American journal of physiology. Renal physiology, 280(2), F244-F253 (2001-02-24)
Because proteinuria has been demonstrated in patients with autosomal-dominant polycystic kidney disease (ADPKD), we have investigated whether proteinuria also occurs in the (cy/+) rat, a widely used model for ADPKD. Increased urinary excretion of proteins, in particular of albumin, can
IgY: clues to the origins of modern antibodies
Warr G W, et al.
Immunology Today, 16(8), 392-398 (1995)
Kerstin Schäfer et al.
Current biology : CB, 30(5), 840-853 (2020-02-23)
Twin arginine translocation (TAT) pathways have been extensively studied in bacteria and chloroplasts for their role in membrane translocation of folded proteins. However, an increasing number of organisms have been found to contain mitochondria-located TAT subunits, including plant mitochondria, which
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