推薦產品
生物源
human
品質等級
化驗
>90% (SDS-PAGE)
形狀
liquid
製造商/商標名
Calbiochem®
儲存條件
OK to freeze
avoid repeated freeze/thaw cycles
運輸包裝
wet ice
儲存溫度
−70°C
一般說明
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.
包裝
Please refer to vial label for lot-specific concentration.
警告
Toxicity: Standard Handling (A)
外觀
In PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
重構
Following initial thaw, aliquot and freeze (-70°C).
其他說明
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.
法律資訊
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
儲存類別代碼
12 - Non Combustible Liquids
水污染物質分類(WGK)
WGK 1
閃點(°F)
Not applicable
閃點(°C)
Not applicable
分析證明 (COA)
輸入產品批次/批號來搜索 分析證明 (COA)。在產品’s標籤上找到批次和批號,寫有 ‘Lot’或‘Batch’.。
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
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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