推荐产品
形式
liquid
制造商/商品名称
Upstate®
技术
affinity chromatography: suitable
immunoprecipitation (IP): suitable
western blot: suitable
运输
wet ice
一般描述
蛋白质A是一种免疫球蛋白(Ig)结合蛋白，用于纯化大量IgG。它与抗体的Fc部分在CH2–CH3界面结合。蛋白质A-琼脂糖可用于低压抗体分离。
重组蛋白A，共价结合到高度交叉链接的6%琼脂糖磁珠。
结合量 40mg 人 IgG/ml 琼脂糖
重组蛋白A，共价结合到高度交叉链接的6%琼脂糖磁珠。
结合量 40mg 人 IgG/ml 琼脂糖
应用
蛋白A琼脂糖，Fast Flow已被用于免疫沉淀和染色质免疫沉淀(ChIP)。
质量
在免疫沉淀中进行了常规评估
外形
含有 0.01％ 硫柳汞的无菌蒸馏水
法律信息
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
Simon Schenk et al.
American journal of physiology. Endocrinology and metabolism, 291(2), E254-E260 (2006-05-04)
Although the increase in fatty acid oxidation after endurance exercise training has been linked with improvements in insulin sensitivity and overall metabolic health, the mechanisms responsible for increasing fatty acid oxidation after exercise training are not completely understood. The primary
Ghia M Euskirchen et al.
Genome research, 17(6), 898-909 (2007-06-15)
Recent progress in mapping transcription factor (TF) binding regions can largely be credited to chromatin immunoprecipitation (ChIP) technologies. We compared strategies for mapping TF binding regions in mammalian cells using two different ChIP schemes: ChIP with DNA microarray analysis (ChIP-chip)
Lei Jiang et al.
Investigative ophthalmology & visual science, 61(5), 41-41 (2020-05-24)
To identify the pathogenic gene of infantile nystagmus syndrome (INS) in three Chinese families and explore the potential pathogenic mechanism of FERM domain-containing 7 (FRMD7) mutations. Genetic testing was performed via Sanger sequencing. Western blotting was used to analyze protein
Vasavi Sundaram et al.
Genome research, 24(12), 1963-1976 (2014-10-17)
Transposable elements (TEs) have been shown to contain functional binding sites for certain transcription factors (TFs). However, the extent to which TEs contribute to the evolution of TF binding sites is not well known. We comprehensively mapped binding sites for
Suzana Markolovic et al.
Nature chemical biology, 14(7), 688-695 (2018-06-20)
Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely related to the JmjC hydroxylases than to the JmjC demethylases. Biophysical
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