应用
该试剂盒旨在最大程度地回收免疫沉淀物。它提供了所有必要的试剂，可从细胞提取物中进行任何蛋白的免疫沉淀，只要该蛋白有适合的抗体。该试剂盒基于蛋白 G，可与最常用的抗体结合。另外，提供了可实现快速洗涤而又不损失蛋白 G 树脂的离心柱，从而使蛋白产量最大化。
特点和优势
- 在洗涤过程中，使得与抗原抗体结合的磁珠损失最小化。
- 通过增加洗涤步骤的严格性，将非特异性信号降至最低，甚至没有。
制备说明
制备试剂时，请使用超纯水（17M -cm）
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Flam. Liq. 3 - Skin Irrit. 2
储存分类代码
3 - Flammable liquids
WGK
WGK 3
法规信息
常规特殊物品
危险化学品
F Gautier et al.
Molecular and cellular biology, 31(4), 832-844 (2010-12-22)
Bcl-2 homologues (such as Bcl-x(L)) promote survival in part through sequestration of "activator" BH3-only proteins (such as Puma), preventing them from directly activating Bax. It is thus assumed that inhibition of interactions between activators and Bcl-x(L) is a prerequisite for
Hubert Arokium et al.
The Journal of biological chemistry, 282(48), 35104-35112 (2007-10-04)
During apoptosis, the pro-apoptotic protein Bax relocalizes from the cytosol to the mitochondrial outer membrane. This relocalization is associated to major conformational changes, namely at the N- and C-terminal ends of the protein. Substitution of residues located at critical positions
R Meller et al.
Cell death and differentiation, 10(5), 539-547 (2003-05-03)
Seizure-induced neuronal death may involve engagement of the BCL-2 family of apoptosis-regulating proteins. In the present study we examined the activation of proapoptotic BAD in cultured hippocampal neurons following seizures induced by removal of chronic glutamatergic transmission blockade. Kynurenic acid
Patricia Workman et al.
Journal of bacteriology, 194(13), 3512-3521 (2012-05-01)
The BamA protein of Escherichia coli plays a central role in the assembly of β-barrel outer membrane proteins (OMPs). The C-terminal domain of BamA folds into an integral outer membrane β-barrel, and the N terminus forms a periplasmic polypeptide transport-associated
Kong-Hung Sze et al.
Cell chemical biology, 24(2), 182-194 (2017-01-24)
Talaromyces (Penicillium) marneffei is one of the leading causes of systemic mycosis in immunosuppressed or AIDS patients in Southeast Asia. How this intracellular pathogen evades the host immune defense remains unclear. We provide evidence that T. marneffei depletes levels of a
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