生物来源
mouse
质量水平
偶联物
unconjugated
抗体形式
purified antibody
抗体产品类型
primary antibodies
克隆
1D10, monoclonal
种属反应性
mouse
技术
RIP: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
western blot: suitable
同位素/亚型
IgG2aκ
NCBI登记号
UniProt登记号
运输
wet ice
靶向翻译后修饰
unmodified
基因信息
mouse ... Rbfox3(52897)
一般描述
免疫原
应用
Epigenetics & Nuclear Function
Nuclear Receptors
Immunohistochemistry Analysis: A representative lot detected Fox1 in coronal sections from E18 mouse (Tang, Z.Z., et al. (2009). Mol Cell Biol. 29(17):4757-4765).
Immunocytochemistry Analysis: A representative lot detected Fox1 in post-mitotic neuronal cells differentiated from mouse embryonal carcinoma P19 cells (Lee, J.A., et al. (2009). Genes Dev. 23(19):2284-2293).
RNA-Binding Protein Immunoprecipitation/iCLIP Analysis: A representative lot was employed to immunoprecipitate Fox1-associated pre-mRNAs from UV-crosslinked murine cortex homogenates by individual-nucleotide resolution crosslinking immunoprecipitation (iCLIP) for characterization of Fox1 pre-mRNA-binding sites (Gehman, L.T., et al. (2011) Nat Genet. 43(7):706-711).
Western Blotting Analysis: A representative lot detected Fox1 in mouse cortical tissue homogenate (Tang, Z.Z., et al. (2009). Mol Cell Biol. 29(17):4757-4765).
外形
制备说明
分析说明
Western Blotting Analysis: 0.5 µg/mL of this antibody detected Fox1 in 10 µg of adult mouse brain tissue lysate.
其他说明
免责声明
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储存分类代码
12 - Non Combustible Liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°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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