conjugate
unconjugated
antibody form
purified antibody
clone
3A6.2, monoclonal
purified by
using protein G
species reactivity
human, mouse
concentration
(Please refer to lot specific datasheet.)
technique(s)
western blot: suitable
isotype
IgG2b
UniProt accession no.
target post-translational modification
unmodified
Quality Level
General description
Application
Physical form
Preparation Note
Analysis Note
Western Blotting Analysis: 2.0 µg/mL of this antibody detected PLGF in 10 µg of HUVEC cell lysate.
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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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