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一般說明
5′-三磷酸腺苷-琼脂糖（5′-ATP-琼脂糖）是5-ATP通过5′-ATP的C-8原子与交联4%珠状琼脂糖形成的缀合物（由溴化氰激活）。5′-ATP–琼脂糖适用于各种蛋白质和酶的亲和纯化，如周期蛋白依赖性激酶2（CDK2）、热休克蛋白和隐花色素。
應用
5′-三磷酸腺苷-琼脂糖（5′-ATP–琼脂糖）适用于各种蛋白质和酶的亲和纯化，如周期蛋白依赖性激酶2（CDK2）、热休克蛋白-70（HSP-70）和隐花色素。5′-ATP琼脂糖已用于亲和色谱中，以从艾氏腹水癌肿瘤细胞中纯化尿苷激酶。
腺苷5′-三磷酸琼脂糖（5′-ATP琼脂糖）已用于亲和色谱中，以从艾氏腹水癌肿瘤细胞中纯化尿苷激酶。
外觀
用乳糖稳定化的冻干粉
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
其他客户在看
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The Journal of biological chemistry, 271(42), 25989-25993 (1996-10-18)
Cysteine string protein (CSP) is a 34 kDa secretory vesicle protein bearing a "J-domain" as well as a palmitoylated cysteine-rich "string" region used for membrane attachment. Mutation of the CSP gene causes impaired presynaptic neuromuscular transmission in Drosophila melanogaster, implicating
M Brungs et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(1), 107-111 (1995-01-03)
5-Lipoxygenase (5-LO; EC 1.13.11.34) activity in the human monocytic cell line Mono Mac 6 was upregulated by combined treatment with transforming growth factor beta 1 (TGF-beta) and 1,25-dihydroxyvitamin D3 (VD3). In undifferentiated cells, 5-LO enzyme activity was undetectable. After the
C Greiner et al.
British journal of pharmacology, 164(2b), 781-793 (2011-04-22)
5-Lipoxygenase (5-LO) is the key enzyme in the biosynthesis of pro-inflammatory leukotrienes (LTs) representing a potential target for pharmacological intervention with inflammation and allergic disorders. Although many LT synthesis inhibitors are effective in simple in vitro test systems, they frequently
L Fischer et al.
British journal of pharmacology, 152(4), 471-480 (2007-08-21)
Licofelone is a dual inhibitor of the cyclooxygenase and 5-lipoxygenase (5-LO) pathway, and has been developed for the treatment of inflammatory diseases. Here, we investigated the molecular mechanisms underlying the inhibition by licofelone of the formation of 5-LO products. The
C Prodromou et al.
The EMBO journal, 18(3), 754-762 (1999-02-02)
The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is dependent on the binding and hydrolysis of ATP, and on interactions with a variety of co-chaperones containing tetratricopeptide repeat (TPR) domains. We have now analysed the
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