产品名称
Anti-RBPJ Antibody, serum, from rabbit
biological source
rabbit
conjugate
unconjugated
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
mouse, human
species reactivity (predicted by homology)
primate (based on 100% sequence homology)
technique(s)
ChIP: suitable (ChIP-seq)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... RBPJ(3516)
Analysis Note
Western Blotting Analysis: A 1:5,000 dilution of this antibody detected RBPJ in 10 µg of HEK293 cell lysate.
Application
Western Blotting Analysis A 1:2,000 dilution from a representative lot detected RBP-J in GM12878 lymphoblasts (Courtesy of Dr Zhao Bo).
ChIP-seq Analysis: A representative lot detected RBP-J in ChIP-seq applications (Wang, H., et. al. (2011). Proc Natl Acad Sci USA. 108(36):14908-13).
Western Blotting Analysis: A representative lot detected RBPJ in T-cell acute lymphoblastic leukemia (T-ALL) cell lines of both human (KOPT-K1 , HPB-ALL, and CUTLL1) and murine (T6E and G4A2) origins) (Wang, H., et. al. (2011). Proc Natl Acad Sci USA. 108(36):14908-13).
Chip-seq Analysis: A representative lot detected RBPJ in GM12878 cells (Courtesy of Dr Zhao Bo).
Epigenetics & Nuclear Function
Nuclear Receptors
Biochem/physiol Actions
Disclaimer
General description
Immunogen
Other Notes
Physical form
Preparation Note
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
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存储类别
10 - Combustible liquids
wgk
WGK 1
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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