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Sigma-Aldrich

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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Synonym(s):
Calmodulin, Human, Recombinant

biological source

human

Quality Level

100

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

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.

Packaging

Please refer to vial label for lot-specific concentration.

Warning

Toxicity: Standard Handling (A)

Physical form

In PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).

Reconstitution

Following initial thaw, aliquot and freeze (-70°C).

Other Notes

Chou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
Lennon, G., et al. 1996.Genomics33, 151.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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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