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A4187

Sigma-Aldrich

Anti-Goat IgG (whole molecule)–Alkaline Phosphatase antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Rabbit Anti-Goat IgG (whole molecule)–AP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

goat

technique(s)

direct ELISA: 1:30,000
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50
western blot: 1:30,000

shipped in

wet ice

storage temp.

2-8°C

target post-translational modification

unmodified

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General description

IgG antibodies regulate several functions such as complement activation and phagocytosis. Thus they play a crucial role in facilitating cytological immune responses. Polyclonal anti-goat IgG (whole molecule)–alkaline phosphatase antibody (diluted 1:15,000) can be used as a secondary antibody for immunoblotting of Sall4. This antibody can also be used in immunohistochemistry (diluted1:400) . Rabbit anti-goat IgG antibody reacts specifically with goat IgG and normal goat serum.
Primary goat antibodies are often used to study target proteins for various clinical and research purposes. Thus, secondary anti-goat antibody conjugated to a detectable substrate can be used to facilitate the accurate detection and localization of target proteins.

Specificity

Binds all goat Igs

Immunogen

Purified goat IgG.

Application

Anti-Goat IgG (whole molecule)-Alkaline Phosphatase antibody is suitable for use in immunoblotting. The product can also be used for direct ELISA (1:30,000) and immunohistochemistry (1:50 using formalin-fixed, paraffin-embedded sections).
Detection of TLR2 and TLR4 in protein extracts from epidermal keratinocytes was performed by western blot using alkaline phosphatase conjugated rabbit anti-goat IgG as the secondary at a 1:2500 dilution.

Physical form

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl2, 1% bovine serum albumin, 50% glycerol and 15 mM sodium azide.

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

10 - Combustible liquids

WGK

WGK 2


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Andor Pivarcsi et al.
International immunology, 15(6), 721-730 (2003-05-17)
Keratinocytes have the ability to kill pathogenic fungi and bacteria by producing antimicrobial substances. Recent studies suggest that microbial components use signaling molecules of the human Toll-like receptor (TLR) family to transduce signals in various cells. Here we provide evidence
Menhaj et al.
Planta, 209(4), 406-413 (1999-11-07)
An antibody was raised against the protein HL#2 which is a nuclear-encoded light-stress-induced protein of barley (Hordeum vulgare L.). The expression of the mRNA and the protein of HL#2 was determined under the influence of high light and methyl jasmonate.
Minoru Omi et al.
The Journal of comparative neurology, 519(13), 2615-2621 (2011-04-15)
The optic tectum is a visual center of nonmammalian vertebrates that receives retinal fibers in a retinotopic manner. It has been accepted that retinal fibers project to some superficial laminae of the tectum, but do not go through lamina g
Jesse L Cox et al.
PloS one, 5(11), e15486-e15486 (2010-11-26)
Master regulators, such as Sox2, Oct4 and Nanog, control complex gene networks necessary for the self-renewal and pluripotency of embryonic stem cells (ESC). These master regulators associate with co-activators and co-repressors to precisely control their gene targets. Recent studies using
György Szláma et al.
The FEBS journal, 280(16), 3822-3839 (2013-07-09)
Myostatin, a negative regulator of skeletal muscle growth, is produced from myostatin precursor by multiple steps of proteolytic processing. After cleavage by a furin-type protease, the propeptide and growth factor domains remain associated, forming a noncovalent complex, the latent myostatin

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