AP160P
Rabbit Anti-Mouse IgG Antibody, HRP conjugate
Chemicon®, from rabbit
Synonym(s):
Rabbit Anti-Mouse Antibody
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.46
Recommended Products
biological source
rabbit
Quality Level
conjugate
peroxidase conjugate
antibody form
F(ab′)2 fragment of affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
species reactivity
mouse
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
western blot: suitable
shipped in
wet ice
target post-translational modification
unmodified
General description
Immunoglobulin G (IgG) is the most abundant glycoprotein antibody found in human serum. It is secreted by the B cells. IgG structure contains four polypeptide chains, which include two identical heavy (H) chains and two identical λ light (L) chains. These chains are inter-linked by disulfide bonds. IgG exists in four isotypes IgG1, IgG2, IgG3, and IgG4.
Application
Rabbit Anti-Mouse IgG Antibody, HRP conjugate has been used in western blotting. (1:2000)(1:200000) (1:5000)
Biochem/physiol Actions
Immunoglobulin G (IgG) aids in the activation of the complement system. It neutralizes virus particles and toxins. IgG facilitates antibody-dependent cell-mediated cytotoxicity (ADCC). Maternal IgG is transferred to the fetus through the placenta that is crucial for protecting newborns against infectious diseases. Detection of IgG levels in severe acute respiratory syndrome coronavirus (SARS‐CoV)‐2 infected patients can be a potential strategy to assess the severity and prognosis of coronavirus disease 2019 (COVID‐19).
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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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Storage Class Code
13 - Non Combustible Solids
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’.
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Elen Rizzi et al.
International journal of cardiology, 165(1), 165-173 (2011-09-16)
Increased oxidative stress upregulates matrix metalloproteinases (MMPs) and transforming grow factor (TGF-β), which are involved in hypertensive cardiac remodeling. We tested the hypothesis that tempol (an antioxidant) could prevent these alterations in two-kidney, one-clip (2K1C) hypertension. Sham-operated or hypertensive rats
Cristina Evangelisti et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 23(12), 4276-4287 (2009-08-29)
MicroRNAs are a class of sophisticated regulators of gene expression, acting as post-transcriptional inhibitors that recognize their target mRNAs through base pairing with short regions along the 3'UTRs. Several microRNAs are tissue specific, suggesting a specialized role in tissue differentiation
Neuron-glia communication: metallothionein expression is specifically up-regulated by astrocytes in response to neuronal injury.
Roger S Chung, Paul A Adlard, Justin Dittmann, James C Vickers, Meng Inn Chuah, Adrian K West
Journal of Neurochemistry null
Rita L Peruquetti et al.
PloS one, 7(8), e42695-e42695 (2012-08-18)
Spermatogenesis is a complex differentiation process that involves genetic and epigenetic regulation, sophisticated hormonal control, and extensive structural changes in male germ cells. RNA nuclear and cytoplasmic bodies appear to be critical for the progress of spermatogenesis. The chromatoid body
Andrezza N Gonçalves et al.
Journal of biotechnology, 157(1), 20-24 (2011-10-18)
Characterization of the matrix metalloproteinase-2 (MMP-2) substrates and understanding of its function remain difficult because up to date preparations containing minor amounts of other eukaryotic proteins that are co-purified with MMP-2 are still used. In this work, the expression of
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