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.
Synonyme(s) :
Calmodulin, Human, Recombinant
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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.
Conditionnement
Please refer to vial label for lot-specific concentration.
Avertissement
Toxicity: Standard Handling (A)
Forme physique
In PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
Reconstitution
Following initial thaw, aliquot and freeze (-70°C).
Autres remarques
Chou, J.J., et al. 2001.Nat. Struct. Biol.8, 990. Lennon, G., et al. 1996.Genomics33, 151.
Informations légales
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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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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