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MilliporeSigma

04-1663

Goat Anti-Mouse IgG Antibody, clone RMG07

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702

Principaux documents

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antibody form

purified antibody

clone

RMG07
monoclonal

purified by

using protein G

species reactivity

mouse

concentration

(Please refer to lot specific datasheet.)

technique(s)

ELISA: suitable

isotype

IgG

Quality Level

300

Analysis Note

ELISA Analysis: The specificity and reactivity of a representative lot was confirmed by ELISA analyses.

Biochem/physiol Actions

This antibody reacts to Mouse IgG, including IgG1, IgG2a, IgG2b, and IgG3. No cross reactivity with IgM, IgA, IgE, human IgG, rat IgG, or rabbit IgG.

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.

General description

Mouse IgG

Physical form

Goat monoclonal in PBS with 1% BSA and 0.09% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.

Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificats d'analyse (COA)

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Contenu apparenté

White Paper: Further considerations of antibody validation and usage.
Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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