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A3562

Sigma-Aldrich

Anti-Mouse IgG (whole molecule)−Alkaline Phosphatase antibody produced in goat

affinity isolated antibody, buffered aqueous glycerol solution

Sinónimos:

Goat Anti-Mouse IgG (whole molecule)−AP

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About This Item

MDL number:
MFCD00162640
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

conjugate

alkaline phosphatase conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

mouse

technique(s)

direct ELISA: 1:30,000
dot blot: 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

Immunoglobulin G (IgG) is a glycoprotein antibody that regulates immune responses such as phagocytosis and is also involved in the development of autoimmune diseases . Mouse IgGs have four distinct isotypes, namely, IgG1, IgG2a, IgG2b, and IgG3. IgG1 regulates complement fixation in mice . Anti-Mouse IgG (whole molecule)-Alkaline Phosphatase antibody is specific for normal mouse serum and mouse IgG. In Ouchterlony double diffusion assays, the antibody reacts with mouse IgG1, IgG2a, IgG2b, IgG3, IgA, and IgM.

Immunogen

Purified mouse IgG

application

Anti-Mouse IgG (whole molecule)-Alkaline Phosphatase antibody is suitable for use in direct ELISA (1:3000) and western blot. The product can also be used for immunohistochemistry (1:50 using formalin-fixed, paraffin-embedded sections).
Surfactant Protein A was detected in bronchoalveolar fluid using alkaline phosphatase conjugated goat anti-mouse IgG as the secondary at μg/ml in TBS/Tween containing final concentration of 0.5M NaCl.

Physical form

Solution in 0.05 M Tris buffer, pH 8.0, containing 1 mM MgCl2, 10 mM glycine, 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

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Peng Li et al.
TheScientificWorldJournal, 2014, 174253-174253 (2014-09-10)
This paper describes the complex effects of postmortem ultimate pH (pHu) on Chinese Yellow crossbreed cattle quality during postmortem ageing and provides an explanation of how pHu affects beef tenderness. High pHu beef had the highest initial tenderness (P <
V Wagh et al.
Cell death & disease, 5, e1320-e1320 (2014-07-11)
FAM40B (STRIP2) is a member of the striatin-interacting phosphatase and kinase (STRIPAK) complex that is involved in the regulation of various processes such as cell proliferation and differentiation. Its role for differentiation processes in embryonic stem cells (ESCs) is till
Jose Velilla et al.
Neurology. Genetics, 5(2), e312-e312 (2019-05-02)
To identify the genetic cause of disease in a form of congenital spinal muscular atrophy and arthrogryposis (CSMAA). A 2-year-old boy was diagnosed with arthrogryposis multiplex congenita, severe skeletal abnormalities, torticollis, vocal cord paralysis, and diminished lower limb movement. Whole-exome
S Munir Alam et al.
Journal of virology, 82(1), 115-125 (2007-10-19)
Two human monoclonal antibodies (MAbs) (2F5 and 4E10) against the human immunodeficiency virus type 1 (HIV-1) envelope g41 cluster II membrane proximal external region (MPER) broadly neutralize HIV-1 primary isolates. However, these antibody specificities are rare, are not induced by
Martin Siegemund et al.
mAbs, 8(5), 879-891 (2016-04-12)
Fusion proteins combining oligomeric assemblies of a genetically obtained single-chain (sc) variant of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) with antibodies directed against tumor-associated antigens represent a promising strategy to overcome the limited therapeutic activity of conventional soluble TRAIL. To
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