DNA分离PS-快速试剂

　　20分钟即可从石蜡包埋组织切片提取DNA的试剂。

◆特点

●　无需脱石蜡处理和蛋白质分解处理。

●　约20分钟即可短时间提取DNA。

●　适用于500bp以下的DNA扩增。

●　混入极微量的PCR抑制剂。

◆组成

　　DNA Isolation Solution・・10mL×5个（眼科滴瓶型管）  ※眼科滴瓶型管1滴约30μL

◆数据

　　以各组织的石蜡包埋切片提取DNA为模板进行β-globin基因扩增。

泌尿·生殖系统作用药成分

◆盐酸黄酮哌酯（Flavoxate   Hydrochloride）

CAS No. 3717-88-2 C24H25NO4・HCl=427.93 纯度:99.0+％（Titration） 可溶性溶剂:水 用途（作用）:对膀胱平滑肌收缩有抑制作用。

◆四氮六甲圜（Hexamethylenetetramine）

CAS No. 100-97-0 C6H12N4=140.19 纯度:99.0+％（Titration） 可溶性溶剂:水 用途（作用）:对泌尿器官有抗菌作用。

◆盐酸羟苄羟麻黄碱（同分异构体混合物）（Ritodrine   Hydrochloride（mixture of isomers））

CAS No. 23239-51-2 C17H21NO3・HCl=323.81 纯度:98.0+％（HPLC） 可溶性溶剂:水 用途（作用）:平滑肌舒缓剂，有舒缓子宫作用，防止流产。

◆枸橼酸西地那非（Sildenafil Citrate）

CAS No. 171599-83-0 C22H30N6O4S・C6H8O7=666.70 纯度:90.0+％（HPLC） 可溶性溶剂:DMSO 用途（作用）:对磷酸二酯酶5（PDE-5）酶活性有抑制作用。

相关资料详情请查看：http:///pdf/show/80.html

Screen-Well^® 肾毒理化合物库

SCREEN-WELL^® Nephrotoxicity library

◆原理

   Enzo Life Sciences提供一系列独一无二的化合物库，包括各类抑制剂、激活剂和诱导剂等各种小分子。随货附送完整的证明书，化合物活性描述、包装规格、化合物浓度含量、物理性状和结构式。方便客户查阅。

◆优点・特色

●   广泛的生产线：提供的化合物库包括FDA批准的化合物，天然产物，受体 de-orphaning化合物，化学基因组学，

     信号通道相关。合计超过2500种化合物，包括天然产物，酶抑制剂，受体的配体，药物，脂类&脂肪酸等。

●   新颖性，化学物库是有相关的小分子组成，Enzo申请专利的

     化合物。

●   简单低成本， 化合物全都溶在相应溶剂中、无需额外溶解

      步骤，即可进行筛选。

   ●   包含无毒对照品，大量毒性明确且毒性不同的化合物

   ●   96孔板包装，溶于DMSO中，即可进行筛选

◆案例・应用

　　包括86种化合物，确认具有多样的肾脏毒性反应，包括肾病止痛剂，间质性肾炎，近端和远端小管，急性肾损伤，慢性肾病等。这些化合物的结构和机理都不同，还包括非毒性的对照。化合物溶解在DMSO中，浓度是10mM，分装在96孔深孔板中。可用于预测毒理学筛选和鉴定方法的研发。

运用：高通量筛选。

试剂盒组分：包括86种确认肾脏毒性反应的化合物。包括非毒性的对照。

规格：100uL/孔。

浓度：DMSO溶液（10mM）

稳定性：收到货物后可在-80℃保存6个月。

无DMSO干细胞冻存液

StemCell Keep

StemCell Keep 是一种高效的玻璃化细胞冻存液，用于灵长类胚胎干细胞（ES）和诱导型多能干细胞（iPS）的保存。

◆特点•优势

    ●    无动物源蛋白、无DMSO；

    ●    通过玻璃化保护ES和iPS细胞；

    ●    可维持干细胞分化能力；

    ●    采用新型冷冻保护剂，可利用玻璃化冷冻技术进行ES和iPS细胞克隆的高效保

           存；

    ●    足够分装100管；

    ●    无细菌、真菌和支原体污染；

    ●    保质期长，4℃下可保存2年

　    * 仅用于科学研究，不能用于临床诊断。

◆案例•应用

冷冻玻璃化

灵长类ES和iPS细胞对冷冻损害非常敏感

●   灵长类ES和iPS细胞用含10% DMSO的冻存液-80℃保存后活性很低

●   灵长类ES和iPS细胞克隆在上述条件下活力很低

                      ↓

通过玻璃化低温保存ES和iPS细胞

●   玻璃化是使液体形成玻璃状物质

●   使用玻璃化溶液悬浮细胞，然后转移到液氮罐防止水分缺失

●   细胞在冷冻过程中被保护

                      ↓

玻璃化技术保存ES和iPS细胞存在的问题

●  由于玻璃化的形成需要高浓度的溶液，高渗透压对细胞有毒性

●  操作时需要快速溶解细胞，以防重结晶

●  操作需要经验丰富的操作人员

                      ↓

常规玻璃化溶液存在的问题

●  大体积(200 μL) 的玻璃化溶液可造成玻璃化条件的不稳定性

●  传统的玻璃化溶液含有DMSO和乙酰胺，DMSO对OCT-4的表达有影响，而乙酰胺被认为是一种致癌物

                      ↓

StemCell Keep是一种新颖的玻璃化溶液，

可改善传统玻璃化溶液存在的问题。

　对比数据

上述实验数据反映了人iPS细胞冻存之后的克隆形成率和复苏率。接种后第一天，以未冷冻保存细胞100%的克隆形成率为对照，DAP213（常用作玻璃化试剂）冻存细胞只有15%的克隆形成率，而StemCell冻存细胞的克隆形成率为80%。接种后第四天，细胞生长为大克隆之后统计细胞的复苏率，StemCell冻存iPS 细胞的复苏率达到62%，明显优于DAP213冻存细胞28%的复苏率。

实验操作步骤　

※ 在具体实验展开之前请先进行预实验。

冻存步骤

1. 在超净台上放置一个装满液氮的保温瓶；

2. 用含0.25%的胰蛋白酶和1mg/mL IV型胶原酶的PBS溶液解离ES/iPS细胞；

* 一个60mm培养皿，细胞达到汇合状态时，约可分装1-5管；

3. 离心，去上清( 需在冰上操作)；

4. 用200μL的StemCell悬浮细胞。将冻存管转移到液氮中放置1分钟；

* 如果玻璃化成功，溶液应呈透明状。

5. 将冻存管转移至液氮罐保存。

复苏步骤

1. 准备含有9mL细胞培养液的离心管，37℃水浴；

   * 一次复苏一管。

2. 将冻存管从液氮罐转移至含有液氮的保温瓶中，在超净台上操作；

3. 迅速添加1mL预热的细胞培养基，用枪头轻轻混匀 ；

4. 将所有的稀释后细胞转移至离心管，离心洗脱细胞；

5. 将细胞转移至培养皿，根据实验操作步骤进行细胞培养。

实验结果

人iPS细胞StemCell冻存复苏之后的分化能力

　　细胞的未分化标记物ALP(A)、OCT-4 (B)、SSEA-4 (C) 和TRA-1-60(D) 染色都为阳性，保持着未分化状态。

蛋白磷酸化研究的预制胶

SuperSep Phos-tag™

　　SuperSep Phos-tag™ 是研究蛋白磷酸化的方法，无需特异性磷酸化抗体或者同位素标记。

◆SuperSep Phos-tag™

　　Phos-tag™ 是一种预制胶，预先加入了50 μmol/L的Phostag™ Acrylamide，打开包装即可直接使用。预制胶中含有锌作为金属离子，在中心凝胶缓冲液中保存稳定性很好，得到的带条结果也很整齐。

　　磷酸化蛋白和非磷酸化蛋白作为不同条带分离。

　　分离后，胶可用于考马斯亮蓝染色，免疫印迹和质谱实验。

已公开的验证蛋白列表，请点击

◆Phos-tag™ SDS-PAGE 的原理

◆在HighWire Search 上搜索到的论文数

◆运用

利用p35的丙氨酸突变体确定Cdk5 激活p35的磷酸化位点

　　p35常见的磷酸化位点是Ser8和Thr138。但是Ser8和Thr138位点往往会发生丙氨酸突变，产生3种突变体（Ser8突变体：S8A，Thr138突变体：T138A，Ser8和Thr138双突变体：2A）。这3种突变体、野生型p35、Cdk5和没有激酶活性的Cdk5都来源于COS-7细胞。这些细胞裂解液用Phos-tag™ SDS-PAGE和Western blotting 进行检测（检测抗体：p35抗体）。

100 μM Phos-tag ™ 丙烯酰胺, 7.5% 聚丙烯酰胺凝胶

可明确磷酸化位点和条带迁移率的关系！

– 泳道1（条带L2和L4）和泳道5（条带M1）：p35在Cdk5的作用下发生了磷酸化；

– 泳道1（条带L2和L4）和泳道3（条带L2和L4）：在无激酶活性Cdk5的作用下，大约有一半p35蛋白在Thr138位点

发生磷酸化，同样在138位发生突变的p35蛋白亦是如此。

– 泳道5 （条带M1）和泳道6（条带L3和L4）：Ser8和Thr138是主要的磷酸化位点；

– 泳道5（条带M1）、泳道7（条带L1和L2）和泳道8（条带M2）：条带M1是Ser8和Thr138都发生磷酸化的条带；

条带M2是只有Ser8磷酸化的条带；条带L1和L2是只有Thr138磷酸化的条带。

※ 条带L1和L3中的X 是不确定哪个位点发生磷酸化的条带；

※ 条带L4是非磷酸化的p35。

【参考文献】

▪ Quantitative Measurement of in Vivo Phosphorylation States of Cdk5 Activator p35 by Phos-tag ™ SDS-PAGE. T. Hosokawa, T. Saito, A. Asada, K. Fukunaga, and S. Hisanaga,Mol. Cell. Proteomics, Jun 2010;9: 1133 – 1143.

【结果提供】

理化学研究所 脑科学综合研究中心 回路功能研究核心 记忆功能研究团队 细川智永（Dr. T. Hosokawa）

首都大学东京 理工学研究科 生命科学专业 神经分子功能研究室 久永真市（Dr. S. Hisanaga）

检测含有Dnmt1磷酸化激酶的片段

我们可以确定在片段中含有目的激酶！

① 采用亲和色谱法从鼠脑提取液中纯化GST-Dnmt1（1-290）结合蛋白

② 使用0.3 M 和1 M NaCl 的DNA 纤维素柱洗脱得到目的蛋白

③ GST-Dnmt1（1-290）作为体外激酶实验的反应底物

④ Phos-tag ™ SDS-PAGE 用于Western blotting，确定迁移条带中每个片段的激酶活性

【参考文献】

▪ The DNA-binding activity of mouse DNA methyltransferase 1 is regulated by phosphorylation with casein kinase 1delta/epsilon. Y. Sugiyama, N. Hatano, N. Sueyoshi, I. Suetake, S. Tajima, E. Kinoshita, E. Kinoshita-Kikuta, T. Koike, and I. Kameshita, Biochem. J.,

【结果提供】

高知大学 综合研究中心 生命、功能物质部门 实验实习机器设施 杉山康宪（Dr. Y. Sugiyama）

香川大学 农学部 应用生物科学科 动物功能生化学研究室 龟下勇（Dr. I. Kameshita）

二维电泳中的应用：分析hnRNP K磷酸化异构体

　　小鼠巨噬细胞J774.1 经LPS 刺激后，裂解细胞，经过免疫沉淀法分离得到hnRNP K。在二维电泳中，一维是IPG 胶，二维是Phos-tag ™ SDS-PAGE，可分离hnRNP K 的异构体。利用质谱仪，可以确认不同的点代表不同的亚型或修饰蛋白。

同一个等电点的位置上，不同位点发生磷酸化都可以被区分开来

（例: spots 6 vs. 8 and spots 4 vs. 7）

【参考文献】

▪ Characterization of multiple alternative forms of heterogeneous nuclear ribonucleoprotein K by phosphate-affinity electrophoresis. Y. Kimura, K. Nagata, N Suzuki, R. Yokoyama, Y. Yamanaka, H. Kitamura, H. Hirano, and O. Ohara, Proteomics, Nov 2010; 10(21): 3884-95.

【结果提供】

横滨市立大学 生命纳米系统科学研究科 生物体超分子系统科学专业 木村弥生（Dr. Y. Kimura）、平野久（Dr. H. Hirano）

理化学研究所RCAI 小原收

◆备注

样品制备：

Phos-tag SDS-PAGE对于蛋白样品中的杂质非常敏感，尤其是螯合剂，钒酸，无机盐，表面活性剂这类物质。

强烈建议在Phos-tag SDS-PAGE之前通过TCA沉淀或渗析法降低杂质含量。

转膜前处理：

另一个必须的步骤是在转膜前，用EDTA去除凝胶中的金属离子（Mn2+或者Zn2+）；

该步骤可提高蛋白的转膜效率。

●　分别准备10 mmol/L 含EDTA和不含EDTA 两种1x transfer buffer。

●　将凝胶浸泡在含10 mmol/L EDTA的1x transfer buffer，至少20分钟，温和摇晃。更换新缓冲液，重复3次。

●　将凝胶浸泡在不含10 mmol/L EDTA的1x transfer buffer，10分钟，温和摇晃。

●　转膜操作*。

* 建议用湿法转膜，以提高转膜效率。

◆质量控制

　　每一批SuperSep Phos-tag™，出厂前均根据其产品规格进行测试，以保证可分离磷酸化和非磷酸化蛋白，以及他们的分离成都在正常参数内。

◆保存温度

2-10℃

◆产品信息

用于Bio-Rad伯乐电泳仪

用于Life Technologies电泳仪

用于Wako EasySeperator电泳仪

◆相关产品

Phos-tag™ 系列

磷酸化蛋白新方法！

　　Phos-tag™是一种能与磷酸离子特异性结合的功能性分子。它可用于磷酸化蛋白的分离（Phos-tag™ Acrylamide）、Western Blot检测（Phos-tag™ Biotin）、蛋白纯化 （Phos-tag™Agarose）及质谱分析MALDI-TOF/MS （Phos-tag™ Mass Analytical Kit）。

◆Phos-tag™ 的基本结构：

特点：

与-2价磷酸根离子的亲和性和选择性高于其它阴离子

在pH 5-8的生理环境下生成稳定的复合物

◆原理：

◆相关应用：

◆相关产品：

phos-tag™由日本广岛大学研究生院医齿药学综合研究科医药分子功能科学研究室开发。

更多产品信息，请点击：http://phos-tag.jp

Phos-tag 第5版说明书

Phos-tag系列 ver 5

【参考文献】

·  Conversion of graded phosphorylation into switch-like nuclear translocation via autoregulatory mechanisms in ERK signalling[J].Nature communications, 2016, 7，Shindo Y, Iwamoto K, Mouri K, et al.

·  PTEN modulates EGFR late endocytic trafficking and degradation by dephosphorylating Rab7[J]. Nature communications, 2016, 7，Shinde S R, Maddika S.

·  Feedback control of ErbB2 via ERK-mediated phosphorylation of a conserved threonine in the juxtamembrane domain[J]. Scientific Reports, 2016, 6: 31502，Kawasaki Y, Sakimura A, Park C M, et al.

·  Plastid-nucleus communication involves calcium-modulated MAPK signalling[J]. Nature Communications, 2016, 7，Guo H, Feng P, Chi W, et al.

·  Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation[J]. Nature communications, 2016, 7，Mitterer V, Murat G, Réty S, et al.

·  Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors[J]. Biochemical Journal, 2016: BCJ20160557，Ito G, Katsemonova K, Tonelli F, et al.

·  Analysis of phosphorylation of the myosin targeting subunit of smooth muscle myosin light chain phosphatase by Phos-tag SDS-PAGE[J]. The FASEB Journal, 2016, 30(1 Supplement): 1209.1-1209.1，Walsh M P, MacDonald J A, Sutherland C.

·  Using Phos-Tag in Western Blotting Analysis to Evaluate Protein Phosphorylation[J]. Kidney Research: Experimental Protocols, 2016: 267-277，Horinouchi T, Terada K, Higashi T, et al.

·  The Abundance of Nonphosphorylated Tau in Mouse and Human Tauopathy Brains Revealed by the Use of Phos-Tag Method[J]. The American journal of pathology, 2016, 186(2): 398-409，Kimura T, Hatsuta H, Masuda-Suzukake M, et al.

·  Phos-tag SDS-PAGE resolves agonist-and isoform-specific activation patterns for PKD2 and PKD3 in cardiomyocytes and cardiac fibroblasts[J]. Journal of Molecular and Cellular Cardiology, 2016，Qiu W, Steinberg S F.

·  Analysis of phosphorylation of the myosin-targeting subunit of myosin light chain phosphatase by Phos-tag SDS-PAGE[J]. American Journal of Physiology-Cell Physiology, 2016, 310(8): C681-C691，Sutherland C, MacDonald J A, Walsh M P.

·  Electrochemical biosensor for protein kinase A activity assay based on gold nanoparticles-carbon nanospheres, phos-tag-biotin and β-galactosidase[J]. Biosensors and Bioelectronics, 2016, 86: 508-515，Zhou Y, Yin H, Li X, et al.

·  Validation of Cis and Trans Modes in Multistep Phosphotransfer Signaling of Bacterial Tripartite Sensor Kinases by Using Phos-Tag SDS-PAGE[J]. PloS one, 2016, 11(2): e0148294，Kinoshita-Kikuta E, Kinoshita E, Eguchi Y, et al.

·  Phosphopeptide Detection with Biotin-Labeled Phos-tag[J]. Phospho-Proteomics: Methods and Protocols, 2016: 17-29，Kinoshita-Kikuta E, Kinoshita E, Koike T.

·  A Phos‐tag SDS‐PAGE method that effectively uses phosphoproteomic data for profiling the phosphorylation dynamics of MEK1[J]. Proteomics, 2016，Kinoshita E, Kinoshita‐Kikuta E, Kubota Y, et al.

·  Difference gel electrophoresis of phosphoproteome: U.S. Patent Application 15/004,339[P]. 2016-1-22，Tao W A, Wang L.

·  ERK1/2-induced phosphorylation of R-Ras GTPases stimulates their oncogenic potential[J]. Oncogene, 2016，Frémin C, Guégan J P, Plutoni C, et al.

·  Microtubules Inhibit E-Cadherin Adhesive Activity by Maintaining Phosphorylated p120-Catenin in a Colon Carcinoma Cell Model[J]. PloS one, 2016, 11(2): e0148574，Maiden S L, Petrova Y I, Gumbiner B M.

·  Serine 231 and 257 of Agamous-like 15 are phosphorylated in floral receptacles[J]. Plant Signaling & Behavior, 2016, 11(7): e1199314，Patharkar O R, Macken T A, Walker J C.

·  A small molecule pyrazolo [3, 4-d] pyrimidinone inhibitor of zipper-interacting protein kinase suppresses calcium sensitization of vascular smooth muscle[J]. Molecular pharmacology, 2016, 89(1): 105-117，MacDonald J A, Sutherland C, Carlson D A, et al.

·  The RNA polymerase II C-terminal domain phosphatase-like protein FIERY2/CPL1 interacts with eIF4AIII and is essential for nonsense-mediated mRNA decay in Arabidopsis[J]. The Plant Cell, 2016: TPC2015-00771-RA，Chen T, Qin T, Ding F, et al.

·  Vasorelaxant Effect of 5′-Methylthioadenosine Obtained from Candida utilis Yeast Extract through the Suppression of Intracellular Ca2+ Concentration in Isolated Rat Aorta[J]. Journal of agricultural and food chemistry, 2016, 64(17): 3362-3370，Kumrungsee T, Akiyama S, Saiki T, et al.

·  Inhibition of deubiquitinating activity of USP14 decreases tyrosine hydroxylase phosphorylated at Ser19 in PC12D cells[J]. Biochemical and biophysical research communications, 2016, 472(4): 598-602，Nakashima A, Ohnuma S, Kodani Y, et al.

·  Actin Tyrosine-53-Phosphorylation in Neuronal Maturation and Synaptic Plasticity[J]. The Journal of Neuroscience, 2016, 36(19): 5299-5313，Bertling E, Englund J, Minkeviciene R, et al.

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·  Quantitative phosphoproteomics of protein kinase SnRK1 regulated protein phosphorylation in Arabidopsis under submergence[J]. Journal of experimental botany, 2016: erw107，Cho H Y, Wen T N, Wang Y T, et al.

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·  Lysophosphatidylcholine acyltransferase 1 protects against cytotoxicity induced by polyunsaturated fatty acids[J]. The FASEB Journal, 2016, 30(5): 2027-2039，Akagi S, Kono N, Ariyama H, et al.

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·  Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiae[J]. Genetics, 2016: genetics. 115.183939，Paulissen S M, Slubowski C J, Roesner J M, et al.

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·  Intergenic VNTR Polymorphism Upstream of rocA Alters Toxin Production and Enhances Virulence in Streptococcus pyogenes[J]. Infection and immunity, 2016: IAI. 00258-16，Zhu L, Olsen R J, Horstmann N, et al.

·  Ajuba Phosphorylation by CDK1 Promotes Cell Proliferation and Tumorigenesis[J]. Journal of Biological Chemistry, 2016: jbc. M116. 722751，Chen X, Stauffer S, Chen Y, et al.

·  Editorial: International Plant Proteomics Organization (INPPO) World Congress 2014[J]. Frontiers in Plant Science, 2016, 7，Heazlewood J L, Jorrín-Novo J V, Agrawal G K, et al.

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·  A multiple covalent crosslinked soft hydrogel for bioseparation[J]. Chemical Communications, 2016, 52(15): 3247-3250，Liu Z, Fan L, Xiao H, et al.

·  Advances in crop proteomics: PTMs of proteins under abiotic stress[J]. Proteomics, 2016, 16(5): 847-865，Wu X, Gong F, Cao D, et al.

·  Cyclin-Dependent Kinase Co-Ordinates Carbohydrate Metabolism and Cell Cycle in S. cerevisiae[J]. Molecular cell, 2016, 62(4): 546-557，Zhao G, Chen Y, Carey L, et al.

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References on Phos-tag™ Chemistry

• Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of phosphorylated compounds using a novel phosphate capture molecule, Rapid Communications of Mass Spectrometry, 17, 2075-2081 (2003), H. Takeda, A. Kawasaki, M. Takahashi, A. Yamada, and T. Koike 

• Recognition of phosphate monoester dianion by an alkoxide-bridged dinuclear zinc (II) complex, Dalton Transactions, 1189-1193 (2004), E. Kinoshita, M. Takahashi, H. Takeda, M. Shiro, and T. Koike

• Quantitative analysis of lysophosphatidic acid by time-of-flight mass spectrometry using a phosphate capture molecule, Journal of Lipid Research, 45, 2145-2150 (2004), T. Tanaka, H. Tsutsui, K. Hirano, T. Koike, A. Tokumura, and K. Satouchi

•  Production of 1,2-Didocosahexaenoyl Phosphatidylcholine by Bonito Muscle Lysophosphatidylcholine/Transacylase, Journal of Biochemistry,136, 477-483 (2004), K. Hirano, H. Matsui, T. Tanaka, F. Matsuura, K. Satouchi, and T. Koike

• Novel immobilized zinc(II) affinity chromatography for phosphopeptides and phosphorylated proteins, Journal of Separation Science, 28, 155-162 (2005), E. Kinoshita, A. Yamada, H. Takeda, E. Kinoshita-Kikuta, and T. Koike

• Detection and Quantification of On-Chip Phosphorylated Peptides by Surface Plasmon Resonance Imaging Techniques Using a Phosphate Capture Molecule, Analytical Chemistry, 77, 3979-3985 (2005), K. Inamori, M. Kyo, Y. Nishiya, Y. Inoue, T. Sonoda, E. Kinoshita, T. Koike, and Y. Katayama

• Phosphate-binding tag: A new tool to visualize phosphorylated proteins, Molecular & Cellular Proteomics, 5, 749-757 (2006), E. Kinoshita, E. Kinoshita-Kikuta, K. Takiyama, and T. Koike

• Enrichment of phosphorylated proteins from cell lysate using phosphate-affinity chromatography at physiological pH, Proteomics, 6, 5088-5095 (2006), E. Kinoshita-Kikuta, E. Kinoshita, A. Yamada, M. Endo, and T. Koike

• Separation of a phosphorylated histidine protein using phosphate affinity polyacrylamide gel electrophoresis, Analytical Biochemistry, 360, 160-162 (2007), S. Yamada, H. Nakamura, E. Kinoshita, E. Kinoshita-Kikuta, T. Koike, and Y. Shiro

• Label-free kinase profiling using phosphate-affinity polyacrylamide gel electrophresis, Molecular & Cellular Proteomics, 6, 356-366 (2007), E. Kinoshita-Kikuta, Y. Aoki, E. Kinoshita, and T. Koike

• A SNP genotyping method using phosphate-affinity polyacrylamide gel electrophoresis, Analytical Biochemistry, 361, 294-298 (2007), E. Kinoshita, E. Kinoshita-Kikuta, and T. Koike (The phosphate group at DNA-terminal is efficiently captured by Zn²⁺.Phos-tag.)

• Identification on Membrane and Characterization of Phosphoproteins Using an Alkoxide-Bridged Dinuclear Metal Complex as a Phosphate-Binding Tag Molecule, Journal of Biomolecular Techniques, 18, 278-286 (2007), T. Nakanishi, E. Ando, M. Furuta, E. Kinoshita, E. Kikuta-Kinoshita, T. Koike, S. Tsunasawa, and O. Nishimura

• A mobility shift detection method for DNA methylation analysis using phosphate affinity polyacrylamide gel electrophoresis, Analytical Biochemistry, 378, 102-104 (2008), E. Kinoshita-Kikuta, E. Kinoshita, and T. Koike

• Separation of phosphoprotein isotypes having the same number of phosphate groups using phosphate- affinity SDS-PAGE, Proteomics, 8, 2994-3003 (2008), E. Kinoshita, E. Kinoshita-Kikuta, M. Matsubara, S. Yamada, H. Nakamura, Y. Shiro, Y. Aoki, K. Okita, and T. Koike

• FANCI phosphorylation functions as a molecular switch to turn on the Fanconi anemia pathway, Nature Structural & Molecular Biology, 15, 1138-1146 (2008), M. Ishiai, H. Kitao, A. Smogorzewska, J. Tomida, A. Kinomura, E. Uchida, A. Saberi, E. Kinoshita, E. Kinoshita-Kikuta, T. Koike, S. Tashiro, S. J. Elledge, and M. Takata

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• Two-dimensional phosphate affinity gel electrophoresis for the analysis of phosphoprotein isotypes , Electrophoresis, 30, 550-559 (2009), E. Kinoshita, E. Kinoshita-Kikuta, M. Matsubara, Y. Aoki, S. Ohie, Y. Mouri, and T. Koike

• Formation of lysophosphatidic acid, a wound-healing lipid, during digestion of cabbage leaves, Bioscience, Biotechnology, and Biochemistry,73, 1293-300 (2009), T. Tanaka, G. Horiuchi, M. Matsuoka, K. Hirano, A. Tokumura, T. Koike, and K. Satouchi

• A Phos-tag-based fluorescence resonance energy transfer system for the analysis of the dephosphorylation of phosphopeptides, Analytical Biochemistry, 388, 235-241, (2009), K. Takiyama, E. Kinoshita, E. Kinoshita-Kikuta, Y. Fujioka, Y. Kubo, and T. Koike

• Phos-tag beads as an immunoblotting enhancer for selective detection of phosphoproteins in cell lysates, Analytical Biochemistry, 389, 83-85, (2009), E. Kinoshita-Kikuta, E. Kinoshita, and T. Koike

• Mobility shift detection of phosphorylation on large proteins using a Phos-tag SDS-PAGE gel strengthened with agarose, Proteomics, 9, 4098- 4101 (2009), E. Kinoshita, E. Kinoshita-Kikuta, H. Ujihara, and T. Koike

• Separation and detection of large phosphoproteins using Phos-tag SDS-PAGE, Nature Protocols, 4, 1513-1521 (2009), E. Kinoshita, E. Kinoshita-Kikuta, and T. Koike

• A clean-up technology for the simultaneous determination of lysophosphatidic acid and sphingosine-1-phosphate by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using a phosphate-capture molecule, Phos-tag, Rapid Communications in Mass Spectrometry, 24, 1075-1084 (2010), J. Morishige, M. Urikura, H. Takagi, K. Hirano, T. Koike, T. Tanaka, and K. Satouchi

• Genotyping and mapping assay of single-nucleotide polymorphisms in CYP3A5 using DNA-binding zinc(II) complexes, Clinical Biochemistry, 43, 302-306 (2010), E. Kinoshita, E. Kinoshita-Kikuta, H. Nakashima, and T. Koike

• The DNA-binding activity of mouse DNA methyltransferase 1 is ragulated phosphorylation with casein kinase 1σ/ε, Biochemical Journal, 427, 489-497 (2010), Y. Sugiyama, N. Hatano, N. Sueyoshi, I. Suetake, S. Tajima, E. Kinoshita, E. Kinoshita-Kikuta, T. Koike, and I. Kameshita

  
  

用于检验生产线的无菌性

　　本产品是粘稠状的大豆酪蛋白消化物培养基，用于检验无菌食品生产线的无菌性。因是易溶于水的粘稠状态，可以快速进行稀释后使用。

◆包装外表

◆培养基组成

1罐（12.5kg）/（60％溶液）　250L
灭菌后的pH值是7.1～7.5

●　酪蛋白胨……4,250g
●　大豆蛋白胨……………750g
●　磷酸二氢钾……625g
●　葡萄糖……………………625g
●　氯化钠…………1,250g
●　纯净水……………………5,000g

◆特点

●　用于医药品的无菌试验，具有高增殖性的SCD（大豆酪蛋白消化物）培养基。

●　粘稠状易溶于水，可以在短时间内彻底溶解

●　在配制时无粉尘，不会给环境造成不良影响

◆使用用途

●　新设立无菌灌装生产线，检验生产线运作前的无菌性
●　无菌灌装生产线的改造后，检验生产线运作前的无菌性
●　对生产线的无菌性进行定期检验
●　检验灭菌装置持续运作性能

◆使用例