biological source
mouse
conjugate
unconjugated
antibody form
purified antibody
antibody product type
primary antibodies
clone
D5, monoclonal
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable, western blot: suitable
isotype
IgG2bκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... CD1D(912)
General description
Immunogen
Application
Apoptosis - Additional
Apoptosis & Cancer
Western Blotting Analysis: A representative lot detected exogenously expressed CD1d in CD1d-transfected C1R human lymphoblastoid cells (Kim, H.S., et al. (1999). J Biol Chem. 274(14):9289-9295).
Immunoprecipitation Analysis: A representative lot immunoprecipitated intact as well as degraded CD1d from human penile urethral epithelial (PURL) cells following C. trachomatis (Kawana, K., et al. (2007). J Biol Chem. 282(10):7368-7375).
Immunoprecipitation Analysis: A representative lot immunoprecipitated exogenously expressed CD1d independent of glycosylation states from lysates of CD1d-transfected FO-1 human melanoma cells (Kim, H.S., et al. (1999). J Biol Chem. 274(14):9289-9295).
Physical form
Preparation Note
Analysis Note
Western Blotting Analysis: 4.0 µg/mL of this antibody detected CD1d in 10 µg of THP-1 cell lysate.
Note: Longer exposure time is needed when using total lysates for Western blotting applications. Membrane preparation or immunoprecipitation can be employed to enrich membrane target proteins prior to Western blotting.
Other Notes
Disclaimer
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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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