EZElisa™小鼠蛋白与C激酶1相互作用（PICK1）EL
ISA试剂盒-EZElisa™ Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA Kit- 询价
- Biogradetech
- 美国
- A-QEK10603-96wells
- 2025年07月12日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
运输过程中保存：2-8℃
- 保质期：
1年
- 英文名：
EZElisa™ Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA Kit
- 库存：
100
- 供应商：
艾美捷科技
EZElisa™小鼠蛋白与C激酶1相互作用（PICK1）ELISA试剂盒，EZElisa™ Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA Kit，蛋白与C激酶1相互作用（PICK1）ELISA试剂盒, Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA Kit
产品名称：EZElisa™小鼠肽酶抑制剂16（PI16）ELISA试剂盒-EZElisa™ Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA Kit
产品货号：A-QEK10603-96wells
产品规格：96wells
Enzyme Immunoassay for the estimation of Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA in serum and plasma, tissue homogenates and other biological fluids.
种属：Mouse
检测方法：比色法
检测范围：0.156-10ng/mL
该EZElisa™小鼠蛋白与C激酶1相互作用（PICK1）ELISA试剂盒ELISA的特点包括：即用即用的操作步骤标准化和高重复性批次之间的一致性准确性和精确性经过七个点的验证，符合金环标准质量ELISA的要求，这是Biogradetech质量的基准标志。EZElisa™ ELISA试剂盒用于评估样品中的特定生物标志物，样品可以是血清
运输过程中保存：2-8℃
点击：EZElisa™小鼠肽酶抑制剂16（PI16）ELISA试剂盒-EZElisa™ Mouse Protein Interacting With C Kinase 1 (PICK1) ELISA Kit更多Biogradetech产品信息价格，货期，产品说明，百度搜“艾美捷科技”进入官网网站，查看具体产品且快速下单。
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文献和实验Combined 3C-ChIP-Cloning (6C) Assay: A Tool to Unravel Protein-Mediated Genome Architecture
between chromatin elements without specifically identifying the protein components that mediate such interactions. Here we describe a detailed protocol for C ombined 3C -C hIP-C loning (6C) technology, which combines multiple techniques to identify the proteins
Phage‐Based Expression Cloning to Identify Interacting Proteins
‐shifting: Techniques for studying protein‐protein interactions. Trends Biochem. Sci. 17:246‐249. Chapline, C., Ramsay, K., Klauck, T., and Jaken, S. 1993. Interaction cloning
Interaction Trap/Two‐Hybrid System to Identify Interacting Proteins
, consisting of the DNA‐binding domain of LexA fused to the probe or bait protein, shown as being unable to activate either of the two reporters. (B ) and (C ) The resulting bait strain has been additionally transformed with an activation domain (act)–fused
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