选择尺寸
关于此项目
immunohistochemistry
western blot
immunohistochemistry: suitable
western blot: suitable
产品名称
Anti-Mineralocorticoid Receptor Antibody, clone 2D6, clone 2D6, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2D6, monoclonal
species reactivity
rat
technique(s)
immunocytochemistry: suitable
immunohistochemistry: suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
rat ... Nr3C2(25672)
Analysis Note
Western Blotting Analysis: A 1:500 dilution of this antibody detected Mineralocorticoid Receptor in 10 µg of rat brain cytosol tissue lysate.
Application
Immunocytochemistry Analysis: A representative lot detected Mineralocorticoid Receptor in mouse kidney (Shibata, S., et al. (2013). Cell Metabolism. 18:660-671).
Western Blotting Analysis: A representative lot detected endogenous Mineralocorticoid Receptor (MR) in rat hippocampal cytosolic preparation and exogenously expressed EGFP-rat MR fusion protein in CHO cells (Gomez-Sanchez, C.E., et al. (2006). Endocrinology. 147(3):1343-1348).
Western Blotting Analysis: A representative lot detected endogenous Mineralocorticoid Receptor (MR) in mouse kidney cytosolic fraction and exogenously expressed human MR in COS-7 cells (Shibata, S., et al. (2013) Cell Metab. 18(5):660-671)
Signaling
Signaling Neuroscience
Biochem/physiol Actions
Disclaimer
General description
Immunogen
Other Notes
Physical form
Preparation Note
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
相关内容
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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