选择尺寸
关于此项目
western blot
western blot: suitable
产品名称
Anti-CGI-58 Antibody, serum, from rabbit
Quality Level
biological source
rabbit
conjugate
unconjugated
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
mouse
technique(s)
immunocytochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
mouse ... Abhd5(67469)
Analysis Note
Western Blotting Analysis: A 1:1,000 of this antibody detected CGI-58 in 10 µg of differentiated 3T3-L1 adipocytes cell lysate.
Application
Western Blotting Analysis: A representative lot detected recombinant CGI-58, as well as endogenous CGI-58 in differentiated 3T3-L1 adipocytes, and 3T3-L1 preadipocytes stably expressing ectopic perilipin A or perilipin B (Subramanian, V., et al. (2004). J. Biol. Chem. 279(40):42062-42071).
Immunocytochemistry Analysis: A representative lot detected CGI-58 in 3T3-L1 adipocytes, 3T3-L1 preadipocytes stably expressing perilipin A (Subramanian, V., et al. (2004). J. Biol. Chem. 279:42062-42071).
Western Blotting Analysis: A representative lot detected CGI-58 in mouse cardiac muscle, liver, white and brown adipose tissue (Zierler, K.A., et al. (2013). J. Biol. Chem. 288(14):9892-9904).
Western Blotting Analysis: A representative lot detected CGI-58 in in mouse OP9 adipocytes and brown adipose tissue (Skinner, J.R., et al. (2013). Adipocyte. 2(2):80-86).
Signaling
Signaling Neuroscience
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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