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Merck

A3562

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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UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
Conjugate:
alkaline phosphatase conjugate
Clone:
polyclonal
Application:
DB, ELISA (d), IHC (p), WB
Citations:
194
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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

Quality Level

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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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Clase de almacenamiento

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Scott E Gygax et al.
Genetics, 169(3), 1391-1402 (2005-01-18)
SepB is an essential, conserved protein required for chromosomal DNA metabolism in Aspergillus nidulans. Homologs of SepB include yeast Ctf4p and human hAnd-1. Molecular and bioinformatic characterization of these proteins suggests that they act as molecular scaffolds. Furthermore, recent observations
G Ortiz-Colón et al.
Journal of animal science, 87(6), 1913-1920 (2009-03-03)
Understanding preadipocyte differentiation in economically important adipose depots will facilitate efforts to selectively increase intramuscular (i.m.) lipid accretion in cattle. The objectives of this study were to determine if glucocorticoid receptor (GR) expression differs among bovine stromal-vascular (S-V) cells derived
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
Radeekorn Akkarawongsa et al.
Antimicrobial agents and chemotherapy, 53(3), 987-996 (2008-12-24)
The 773-residue ectodomain of the herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) has been resistant to the use of mutagenic strategies because the majority of the induced mutations result in defective proteins. As an alternative strategy for the
Martina Maric et al.
Journal of virology, 85(19), 9667-9679 (2011-07-22)
Herpes simplex virus 1 (HSV-1) capsids leave the nucleus by a process of envelopment and de-envelopment at the nuclear envelope (NE) that is accompanied by structural alterations of the NE. As capsids translocate across the NE, transient primary enveloped virions

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