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76085

Sigma-Aldrich

Anti-Mouse IgG - Atto 594 antibody produced in goat

~1 mg/mL protein, affinity isolated antibody

Synonym(s):

Atto 594 - goat-Anti-mouse IgG

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

goat

conjugate

Atto 594 conjugate

antibody form

affinity isolated antibody

antibody product type

secondary antibodies

clone

polyclonal

contains

50% glycerol as stabilizer

species reactivity

mouse

concentration

~1 mg/mL protein

fluorescence

λex 603 nm; λem 625 nm in PBS

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

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.
Affinity isolated antigen specific antibody is purified from goat anti-mouse IgG antiserum to remove essentially all goat serum proteins, including immunoglobulin. Goat anti-mouse IgG associates with mouse IgGs.

Immunogen

purified mouse IgG

Application

Atto 594-goat anti-mouse IgG can be used for fluorescence-based immunoassays.

Analysis Note

unconjugated dye ≤5% of total fluorescence; dye-to-protein ratio ≥2

Legal Information

This product is for Research use only. In case of intended commercialization, please contact the IP-holder (ATTO-TEC GmbH, Germany) for licensing.

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 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


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Charles Bou-Nader et al.
Cell host & microbe, 29(9), 1421-1436 (2021-08-14)
The HIV-1 virion structural polyprotein, Gag, is directed to particle assembly sites at the plasma membrane by its N-terminal matrix (MA) domain. MA also binds to host tRNAs. To understand the molecular basis of MA-tRNA interaction and its potential function
Mirko Cortese et al.
Cell host & microbe, 28(6), 853-866 (2020-11-28)
Pathogenesis induced by SARS-CoV-2 is thought to result from both an inflammation-dominated cytokine response and virus-induced cell perturbation causing cell death. Here, we employ an integrative imaging analysis to determine morphological organelle alterations induced in SARS-CoV-2-infected human lung epithelial cells.
Barbara Storti et al.
Computational and structural biotechnology journal, 19, 6140-6156 (2021-11-09)
We exploited a multi-scale microscopy imaging toolbox to address some major issues related to SARS-CoV-2 interactions with host cells. Our approach harnesses both conventional and super-resolution fluorescence microscopy and easily matches the spatial scale of single-virus/cell checkpoints. After its validation
Edward M Courchaine et al.
Cell, 184(14), 3612-3625 (2021-06-12)
Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the "survival of motor neuron protein" (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN's globular
Shun Hang Chan et al.
Developmental cell, 49(6), 867-881 (2019-06-19)
The awakening of the genome after fertilization is a cornerstone of animal development. However, the mechanisms that activate the silent genome after fertilization are poorly understood. Here, we show that transcriptional competency is regulated by Brd4- and P300-dependent histone acetylation

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