A7539
Anti-Rabbit IgG (whole molecule)–Alkaline Phosphatase antibody produced in goat
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Goat Anti-Rabbit IgG (whole molecule)–AP
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About This Item
UNSPSC Code:
12352203
MDL number:
biological source
goat
conjugate
alkaline phosphatase conjugate
antibody form
affinity isolated antibody
antibody product type
secondary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
rabbit
should not react with
human
technique(s)
direct ELISA: 1:1,000
shipped in
wet ice
storage temp.
2-8°C
target post-translational modification
unmodified
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General description
IgGs are glycoprotein antibodies that modulate several immune responses. Rabbit IgGs against target proteins are often used as primary antibodies in various research applications. Thus, secondary anti-rabbit IgGs conjugated to a detectable substrate are useful tools for the analysis of target proteins.
Goat anti-rabbit IgG-alkaline phosphatase antibody binds all rabbit Igs and does not cross react with human serum proteins.
Goat anti-rabbit IgG-alkaline phosphatase antibody binds all rabbit Igs and does not cross react with human serum proteins.
Immunogen
purified rabbit IgG
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Citrullination of antithrombin by PADI4 was analyzed by ELISA using alkaline phosphatase conjugated goat anti-rabbit IgG as the secondary diluted at 1:5000 in 0.05M carbonate/bicarbonate buffer (Ph 9.6).
Goat anti-rabbit IgG-alkaline phosphatase antibody has been used for immunocytochemistry and western blotting (1:1,000) applications. The product may also be used for direct ELISA at 1:1,000.
Western blot analysis of TRAP expression after viral transduction in Sf9 cells was performed using alkaline phosphatase-conjugated goat anti-rabbit IgG as the secondary at 1:500.
Physical form
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2 and 15 mM sodium azide
Other Notes
Antibody adsorbed with human serum proteins
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
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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J L Ried et al.
Plant physiology, 93(2), 662-667 (1990-06-01)
Germination of embryonic axes from dormant grain is inhibited by low concentrations of abscisic acid (ABA) compared with axes from nondormant grain. Incubation of dormant grain axes in 0.05 to 50 micromolar ABA caused the prolonged synthesis of a set
Shaoping Lu et al.
Plant biotechnology journal, 11(3), 380-389 (2013-01-03)
The activation of phospholipase Dα1 (PLDα1) produces lipid messenger phosphatidic acid and promotes stomatal closure in Arabidopsis. To explore the use of the PLDα1-mediated signalling towards decreasing water loss in crop plants, we introduced Arabidopsis PLDα1 under the control of
José Alage Baldé et al.
Journal of plant physiology, 163(1), 19-25 (2005-12-20)
Fusarium oxysporum f. sp. melonis is a highly specialized fungus that attacks the root system of melon (Cucumis melo L.). In this work the presence of a class III chitinase was examined by immunological techniques in the root and stem
William T Hay et al.
Journal of plant physiology, 212, 58-68 (2017-03-09)
Soybean C3 photosynthesis can suffer a severe loss in efficiency due to photorespiration and the lack of a carbon concentrating mechanism (CCM) such as those present in other plant species or cyanobacteria. Transgenic soybean (Glycine max cv. Thorne) plants constitutively
Jenny Ljusberg et al.
The Journal of biological chemistry, 280(31), 28370-28381 (2005-06-03)
Tartrate-resistant acid phosphatase (TRAP) is a metallophosphoesterase participating in osteoclast-mediated bone turnover. Activation of TRAP is associated with the redox state of the di-iron metal center as well as with limited proteolytic cleavage in an exposed loop domain. The cysteine
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