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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

Synonyme(s) :

Goat Anti-Mouse IgG (whole molecule)−AP

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

goat

Conjugué

alkaline phosphatase conjugate

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

secondary antibodies

Clone

polyclonal

Forme

buffered aqueous glycerol solution

Espèces réactives

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

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

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.

Immunogène

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.

Forme physique

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.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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