氨基甙类抗生物质

◆正泰霉素（Gentamicin   Sulfate）

◆硫酸卡那霉素（Kanamycin Sulfate）

◆硫酸新霉素（Neomycin   Sulfate）

◆链霉素硫酸盐（Streptomycin   Sulfate）

◆硫酸阿米卡星（Amikacin   Sulfate）

◆硫酸核糖霉素（Ribostamycin   Sulfate）

相关资料详情请查看：http:///pdf/show/80.html

Phos-tag™ Biotin

无特异性磷酸化抗体时的最佳选择！

　　Phos-tag™ Biotin是与生物素结合的Phos-tag™，可用于免疫印迹法检测磷酸化蛋白。Phos-tag™ Biotin BTL-104和BTL-105可灵敏检测PVDF膜上的磷酸化蛋白。

◆原理

◆优点、特色

●  无辐射。

●  无需PVDF膜的封闭处理。

●  Phos-tag™ 的特异性结合与氨基酸种类、序列无关。

●  可适用于免疫印迹和质谱分析等后续工作。

●   Phos-tag™ BTL母液可稳定保存至少6个月。

●  实验流程与使用HRP标记抗体相类似。

※BTL-104、BTL-105、BTL-111三者连接链（Linker）长度不一，但使用上基本相同。BTL-111灵敏度最高。

◆案例、应用

【使用例：在PVDF 膜上检测磷酸化蛋白】

　　转印在PVDF 膜上的磷酸化蛋白可精确检测到ng级水平，没有检测到相应的去磷酸化蛋白与非磷酸化蛋白的信号斑点。

　　免疫印迹检测磷酸化蛋白——Phos-tag ™ 生物素。

　　摘自Eiji Kinoshita ,et al., Mol.Cel.Proteomics (2006) 5: 749

【使用例：Phos-tag™ 生物素在检测蛋白激酶活性的微阵列（生物芯片）中的运用】

　　蛋白激酶是很多疾病诊断和药物筛选的靶标。近来有科研人员研发了一种检测胞内蛋白激酶活性的高灵敏度多肽微阵列。用微阵列点样机点样2nL体积的底物多肽溶液，使多肽固定在戊二醛预修饰的高氨基末端载玻片。

　　当多肽经细胞裂解液磷酸化后，用荧光标记的抗phosphotyrosine（磷酸化酪氨酸）抗体检测酪氨酸激酶，或者用Phos-tag™ 生物素，接着用荧光标记的亲和素检测丝氨酸或者苏氨酸激酶。之后用自动微阵列扫描仪检测荧光信号。多肽微阵列系统包括简单的多肽固定，只需少量样品，具有高密度阵列。重要的是，检测细胞裂解液蛋白激酶活性的灵敏度高。

　　因此多肽微阵列系统可用于高通量筛选细胞内激酶活性，可用于药物筛选和疾病诊断。

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

Q： BTL-104和BTL-111的区别？

A： BTL-104的溶解度更高，BTL-111的灵敏度更高。

Q： 检测灵敏度达到什么水平？

A： 可达到ng级别。需要使用化学发光试剂，比如ImmunoStar LD(Wako)。

Q： 使用该产品还需要别的试剂或则耗材吗？

A： 硝酸锌（Zn(NO₃)₂）溶液和亲和素标记的HRP（(GE Healthcare Bio-Sciences:       RPN1231)。制备Phos-tag™生物素与亲和素标记的HRP偶联物时需要使用离心过  滤装置(NMWL = 30,000, Nanosep™ 30K, Pall Life Sciences).

Q： Phos-tag^™生物素使用的次数？

A： 主要决定于使用次数和使用量，以下实验次数仅作参考：

     BTL-104：130~1300次；

      BTL-111 1mM溶液：10~100次。

Q： 可测定磷酸化蛋白？

A： 根据条带的浓度，可进行半定量分析。

Q： 能够确定结合磷酸化基团的数目？

A： 不能。

Q： 能否剥除（strip）Phos-tag™生物素？

A： 可以。与含有62.5mM Tris-HCl（pH6.8），2%（w/v）SDS和0.1M 2-巯基乙醇溶液  混合后，震荡15分钟。用1×TBS-T洗涤3次，每次10分钟。

Q： 推荐使用哪种膜？

A： 建议使用PVDF膜。

Q： 使用Phos-tag™ 生物素是否需要封闭？

A： 不需要。封闭会降低检测灵敏度。

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·  Characterization of the Neospora caninum NcROP40 and NcROP2Fam-1 rhoptry proteins during the tachyzoite lytic cycle[J]. Parasitology, 2016, 143(01): 97-113，Pastor-Fernandez I, Regidor-Cerrillo J, Jimenez-Ruiz E, et al.

·  Transcriptional Profile during Deoxycholate-Induced Sporulation in a Clostridium perfringens Isolate Causing Foodborne Illness[J]. Applied and environmental microbiology, 2016, 82(10): 2929-2942，Yasugi M, Okuzaki D, Kuwana R, et al.

·  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.

·  DDK dependent regulation of TOP2A at centromeres revealed by a chemical genetics approach[J]. Nucleic Acids Research, 2016: gkw626，Wu K Z L, Wang G N, Fitzgerald J, et al.

·  OVATE Family Protein 8 Positively Mediates Brassinosteroid Signaling through Interacting with the GSK3-like Kinase in Rice[J]. PLoS Genet, 2016, 12(6): e1006118，Yang C, Shen W, He Y, et al.

·  Epithelial Sel1L is required for the maintenance of intestinal homeostasis[J]. Molecular biology of the cell, 2016, 27(3): 483-490， Sun S, Lourie R, Cohen S B, et al.

·  Effect of Sodium Dodecyl Sulfate Concentration on Supramolecular Gel Electrophoresis[J]. ChemNanoMat, 2016，Tazawa S, Kobayashi K, Yamanaka M.

·  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.

·  Phosphoinositide kinase signaling controls ER-PM cross-talk[J]. Molecular biology of the cell, 2016, 27(7): 1170-1180，Omnus D J, Manford A G, Bader J M, et al.

·  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.

·  Carbon Monoxide Gas Is Not Inert, but Global, in Its Consequences for Bacterial Gene Expression, Iron Acquisition, and Antibiotic Resistance[J]. Antioxidants & redox signaling, 2016，Wareham L K, Begg R, Jesse H E, et al.

·  Two-layer regulation of PAQR3 on ATG14-linked class III PtdIns3K activation upon glucose starvation[J]. Autophagy, 2016: 1-2，Xu D, Wang Z, Chen Y.

·  Regulation of sphingolipid biosynthesis by the morphogenesis checkpoint kinase Swe1[J]. Journal of Biological Chemistry, 2016, 291(5): 2524-2534，Chauhan N, Han G, Somashekarappa N, et al.

·  PAX5 tyrosine phosphorylation by SYK co-operatively functions with its serine phosphorylation to cancel the PAX5-dependent repression of BLIMP1: A mechanism for antigen-triggered plasma cell differentiation[J]. Biochemical and biophysical research communications, 2016, 475(2): 176-181，Inagaki Y, Hayakawa F, Hirano D, et al.

·  A Combined Computational and Genetic Approach Uncovers Network Interactions of the Cyanobacterial Circadian Clock[J]. Journal of Bacteriology, 2016: JB. 00235-16，Boyd J S, Cheng R R, Paddock M L, et al.

·  HuR mediates motility of human bone marrow-derived mesenchymal stem cells triggered by sphingosine 1-phosphate in liver fibrosis[J]. Journal of Molecular Medicine, 2016: 1-14，Chang N, Ge J, Xiu L, et al.

·  Combined replacement effects of human modified β-hexosaminidase B and GM2 activator protein on GM2 gangliosidoses fibroblasts[J]. Biochemistry and Biophysics Reports, 2016，Kitakaze K, Tasaki C, Tajima Y, et al.

·  Roseotoxin B Improves Allergic Contact Dermatitis through a Unique Anti-inflammatory Mechanism Involving Excessive Activation of Autophagy in Activated T-Lymphocytes[J]. Journal of Investigative Dermatology, 2016，Wang X, Hu C, Wu X, et al.

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

  
  

无动物源胰蛋白酶EDTA

　　本品是已经过病原体、内毒素和无菌检测的胰蛋白酶EDTA溶液，可用于贴壁细胞的剥离、各组织的细胞分散等。

　　本品以重组胰蛋白酶为原料，不含动物源物质，无需担心病毒污染，能让您更安心地进行实验。使用方法与0.05%胰蛋白酶-EDTA溶液一样。

◆特点：

　● 不含动物源物质

　● 高细胞剥离率，剥离后细胞生存率高

●产品规格项目：

●细胞剥离能力：

●继代培养时的影响：

查看相关产品请看相关资料

◆ 相关产品：

● 胰蛋白酶EDTA（使用猪细小病毒原料）

● 重组胰蛋白酶

稳固Flask，整齐收纳的中间容器

培养瓶运输收纳盒

iP-TEC Flask专用，运输用中间密闭容器（可高压灭菌）。外观整洁，有2个托盘。

　　① 该运输盒最多可收纳6个Flask

　　可高压灭菌

　　4个带硅胶锁扣，可密封

　　② 稳固iP-TEC Flask的专用托盘

　　可高温灭菌，聚丙烯制

　　③ 防震性与吸液性兼备的吸液片

　　可高温灭菌，100%纤维素

◆产品规格

※套装内容：活细胞运输用盒子1个、专用托盘2个、吸液片6片

※运输盒尺寸（mm）：W210×D147×H70

※运输盒容积：1.3L

※运输盒本体·盖子·托盘：聚苯乙烯     填充物：硅胶     吸液片：纤维素