产品名称
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.
biological source
human
assay
>90% (SDS-PAGE)
form
liquid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
shipped in
wet ice
storage temp.
−70°C
Quality Level
Disclaimer
Toxicity: Standard Handling (A)
General description
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.
Other Notes
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.
Packaging
Please refer to vial label for lot-specific concentration.
Physical form
In PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
Preparation Note
Following initial thaw, aliquot and freeze (-70°C).
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_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
我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持