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Fortfahren mit
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
mouse, rat
technique(s)
immunohistochemistry: suitable, western blot: suitable
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
mouse ... Ripk1(19766)
1 of 4
Dieser Artikel | |||
|---|---|---|---|
| Quality Level 100 | Quality Level 100 | Quality Level 100 | Quality Level 100 |
| antibody form affinity isolated antibody | antibody form affinity isolated antibody | antibody form purified antibody | antibody form affinity isolated antibody |
| biological source rabbit | biological source rabbit | biological source mouse | biological source rabbit |
| shipped in wet ice | shipped in wet ice | shipped in wet ice | shipped in dry ice |
| technique(s) immunohistochemistry: suitable, western blot: suitable | technique(s) western blot: suitable | technique(s) western blot: suitable | technique(s) immunofluorescence: suitable, immunohistochemistry: suitable, indirect ELISA: suitable, western blot: suitable |
| clone polyclonal | clone polyclonal | clone 3C6.1, monoclonal | clone polyclonal |
General description
Immunogen
Application
Apoptosis & Cancer
Apoptosis - Additional
Physical form
Preparation Note
Analysis Note
Western Blotting Analysis (WB): 1 μg/mL of this antibody detected RIPK1 in rat kidney tissue lysate.
Other Notes
Disclaimer
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Lagerklasse
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Analysenzertifikate (COA)
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Verwandter Inhalt
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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