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一般描述
V5 标签是一个 14 个氨基酸的长肽序列（GKPIPNPLGLGST），来源于猴病毒 5（SV5）的 P 和 V 蛋白上的表位，属于副粘病毒家族。单克隆抗 V5 过氧化物酶偶联物与在转染的哺乳动物细胞中表达或通过体外翻译产生的带有 V5 标签的重组融合蛋白反应。
特异性
识别 V5 标签（GKPIPNPLLGLDST）融合蛋白
应用
适用于免疫印迹。
外形
从含有1%BSA和0.05%MIT的0.01 M磷酸盐缓冲盐溶液（pH 7.4）中冻干
制备说明
制备两步戊二醛方法通过Avrameas, S., et al., Scand.J. Immunol., 8, Suppl. 7, 7 (1978)描述。
用 0.5 mL 无菌蒸馏水复溶。
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警示用语：
Warning
危险声明
危险分类
Skin Sens. 1
储存分类代码
12 - Non Combustible Liquids
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Jordan N Ranum et al.
Nucleic acids research, 52(6), 3199-3212 (2024-02-26)
Productive infections by RNA viruses require faithful replication of the entire genome. Yet many RNA viruses also produce deletion-containing viral genomes (DelVGs), aberrant replication products with large internal deletions. DelVGs interfere with the replication of wild-type virus and their presence
Panayotis C Theodoropoulos et al.
Nature chemical biology, 12(4), 218-225 (2016-02-02)
A hallmark of targeted cancer therapies is selective toxicity among cancer cell lines. We evaluated results from a viability screen of over 200,000 small molecules to identify two chemical series, oxalamides and benzothiazoles, that were selectively toxic at low nanomolar
Shuang Li et al.
iScience, 27(5), 109646-109646 (2024-04-19)
Most advanced colorectal cancer (CRC) patients cannot benefit from targeted therapy due to lack of actionable targets. By mining data from the DepMap, we identified FAM126B as a specific vulnerability in CRC cell lines exhibiting low FAM126A expression. Employing a
Steven F Baker et al.
Cell reports, 24(10), 2581-2588 (2018-09-06)
Adaptation of viruses to their hosts can result in specialization and a restricted host range. Species-specific polymorphisms in the influenza virus polymerase restrict its host range during transmission from birds to mammals. ANP32A was recently identified as a cellular co-factor
Mauricio P Contreras et al.
Science advances, 9(18), eadg3861-eadg3861 (2023-05-03)
Parasites counteract host immunity by suppressing helper nucleotide binding and leucine-rich repeat (NLR) proteins that function as central nodes in immune receptor networks. Understanding the mechanisms of immunosuppression can lead to strategies for bioengineering disease resistance. Here, we show that
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