208670
Calmodulin, His•Tag® Human, Recombinant
Calmodulin, His•Tag Human, Recombinant, is a full-length, recombinant human calmodulin fused to a His•Tag sequence at the N-terminus. Contains four functional Ca2+-binding sites.
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所有图片(1)
别名:
Calmodulin, Human, Recombinant
UNSPSC代码:
12352202
NACRES:
NA.77
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生物来源
human
质量水平
检测方案
>90% (SDS-PAGE)
形式
liquid
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
avoid repeated freeze/thaw cycles
运输
wet ice
储存温度
−70°C
一般描述
Full-length, recombinant human calmodulin fused to a His•Tag sequence at the N-terminus. Contains four functional Ca2+-binding sites (aa 20-31; aa 56-67; aa 93-104; aa 129-140) with EF-hands (aa 7-42; aa 43-78; aa 80-115; aa 116-148); and a ubiquitination site at Lys21. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Through its interaction with Ca2+, calmodulin mediates the control of a large number of enzymes, including protein kinases and phosphatases. It is expected to be phosphorylated at Thr44 by CaMK4. In addition, it serves as a substrate for various protein tyrosine kinases.
包装
Please refer to vial label for lot-specific concentration.
警告
Toxicity: Standard Handling (A)
外形
In PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
重悬
Following initial thaw, aliquot and freeze (-70°C).
其他说明
Chou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
Lennon, G., et al. 1996.Genomics33, 151.
Lennon, G., et al. 1996.Genomics33, 151.
法律信息
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Takahiro Goshima et al.
Scientific reports, 9(1), 12779-12779 (2019-09-06)
The Calcineurin/NFAT (nuclear factor of activated T cells) pathway plays an essential role in the tumorigenic and metastatic properties in breast cancer. The molecular mechanism of the antiproliferative effect of calcineurin inhibition, however, is poorly understood. We found that calcineurin
Takahiro Masaki et al.
Proceedings of the National Academy of Sciences of the United States of America, 118(44) (2021-10-30)
Estrogen receptor α (ER-α) mediates estrogen-dependent cancer progression and is expressed in most breast cancer cells. However, the molecular mechanisms underlying the regulation of the cellular abundance and activity of ER-α remain unclear. We here show that the protein phosphatase
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