ABS1616
Anti-CGI-58 Antibody
serum, from rabbit
别名:
1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (EC:2.3.1.51), Abhydrolase domain-containing protein 5, Lipid droplet-binding protein CGI-58, Protein CGI-58, CGI-58
生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
serum
抗体产品类型
primary antibodies
克隆
polyclonal
种属反应性
mouse
技术
immunocytochemistry: suitable
western blot: suitable
NCBI登记号
UniProt登记号
运输
dry ice
靶向翻译后修饰
unmodified
基因信息
mouse  ...  Abhd5(67469)   
一般描述
免疫原
应用
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
外形
制备说明
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.
分析说明
Western Blotting Analysis: A 1:1,000 of this antibody detected CGI-58 in 10 µg of differentiated 3T3-L1 adipocytes cell lysate.
其他说明
免责声明
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储存分类代码
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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