biological source
rabbit
conjugate
unconjugated
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human, mouse
species reactivity (predicted by homology)
rat (based on 100% sequence homology)
technique(s)
immunocytochemistry: suitable, immunohistochemistry: suitable, immunoprecipitation (IP): suitable, western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... KHDRBS1(10657)
mouse ... Khdrbs1(20218)
rat ... Khdrbs1(117268)
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General description
Immunogen
Application
信号神经科学
信号传导
免疫组化分析:一个代表性批次的1:600 稀释液在小鼠结肠组织中检测到Sam 68(数据由麦吉尔大学Stephane Richard提供)。
蛋白质印迹分析:一个代表性批次在HeLa 细胞的内源性Sam 68 和外源表达的GFP-Sam 68 融合体中检测到Sam 68(Chen, Q., et al. (1999).Mol Biol Cell. 10(9):3015-3033).
蛋白质印迹分析:一个代表性批次在GFP-Sam68转染的HEK293、小鼠皮层、海马体、小脑和小鼠脑中检测到Sam 68(Iijima, T., et al. (2011).Cell. 147(7):1601-1614)。
蛋白质印迹分析:一个代表性批次在GFP-Sam68转染的HeLa细胞、MDA-MB-231、MDA-MB-468和BT20中检测到Sam 68(Lukong, K.E., et al. (2005).J Biol Chem. 280(46):38639-38647)。
蛋白质印迹分析:一个代表性批次在分离的小鼠细胞和小鼠胚胎细胞的裂解液中检测到Sam 68(Richard, S., et al. (2005).PLoS Genet. 1(6):e47)。
免疫组织化学分析:一个代表性批次在小鼠小脑、脑干和小脑旁矢状切面中检测到Sam 68(Iijima, T., et al. (2011).Cell. 147(7):1601-1614)。
免疫组化分析:一个代表性批次在胚胎小鼠中检测到Sam 68(Richard, S., et al. (2005).PLoS Genet. 1(6):e47).
免疫细胞化学分析:一个代表性批次在HeLa细胞中检测到Sam 68(Chen, T., et al. (1999).Mol Biol Cell. 10(9):3015-3033)。
蛋白质印迹分析:一个代表性批次在HeLa细胞、GFP-Sam68转染的HeLa细胞和 MDA-MB-468中检测到Sam 68(Lukong, K.E., et al. (2005).J. Biol. Chem. 280(46):38639-38647)。
Biochem/physiol Actions
Physical form
Preparation Note
使用建议:收货后,在取下瓶盖之前,将小瓶离心并轻轻混合溶液。分装到微量离心管中,并储存于-20°C。避免反复冻融循环,以免损坏IgG和影响产品性能。
Analysis Note
蛋白质印迹分析:该抗体的1:500稀释液在10 µg MDA-MB-468细胞裂物中检测到Sam68。
Other Notes
Disclaimer
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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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