Calcium-binding protein produced in E.coli
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Human recombinant calmodulin (Prod. No. BML-SE325) activation of human calcineurin is essentially identical to that of purified bovine brain calmodulin (native, bovine). Initial rates of calcineurin phosphatase activity were determined as a function of calmodulin concentration with the Calcineurin Colorimetric Drug Discovery Kit (Prod. No. BML-AK804). (Note that the human and bovine calmodulin amino acid sequences are 100% identical.)


Product Details
Alternative Name |
CaM, Phosphodiesterase 3′:5′-cyclic nucleotide activator |
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Application Notes |
Calmodulin can be used to activate calmodulin-dependent phosphodiesterase, calcineurin, CaM kinases, etc. |
Biological Activity |
Elicits Ca2+-dependent activation of calcineurin (Ca2+/calmodulin-dependent Ser/Thr protein phosphatase 2B, PP-2B) with the same potency and to the same maximum extent as purified native calmodulin. |
CAS |
73298-54-1 |
Formulation |
Lyophilized. Salt-free. |
MI |
14: 1719 |
MW |
16.8 kDa |
Purity |
≥95% (SDS-PAGE) |
Purity Detail |
Purified by multi-step chromatography. |
Reconstitution |
Reconstitute in water or an appropriate buffer. |
Sequence |
Sequence identical to Genbank accession M27319.1. |
Source |
Produced in E. coli. |
UniProt ID |
P62158 |
Handling & Storage
Handling |
Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -20°C. |
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Long Term Storage |
-20°C |
Shipping |
Blue Ice |
Regulatory Status |
RUO – Research Use Only |
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- Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer: Yang, X., Ma, X., et al.; Nat. Commun. 16, 1871 (2025), Abstract
- Development of a monoclonal antibody specific for a calpain-generated Δ48 kDa calcineurin fragment, a marker of distressed astrocytes: S.D. Kraner, et al.; J. Neurosci. Methods 402, 110012 (2024), Abstract
- Feed-forward stimulation of CAMK2 by the oncogenic pseudokinase PEAK1 generates a therapeutically ‘actionable’ signalling axis in triple negative breast cancer: Yang, X., Ma, X., et al.; bioRxiv , (2024)
- Synaptic BMAL1 phosphorylation controls circadian hippocampal plasticity: I. Barone, et al.; Sci. Adv. 9, eadj1010 (2023), Abstract
- 1D continuous gel electrophoresis composition for the separation of deamidated proteins: Boudier-Lemosquet, A., Mahler, A., et al.; Methods 200, 23 (2022), Abstract
- Calcineurin dephosphorylates topoisomerase IIβ and regulates the formation of neuronal-activity-induced DNA breaks: Delint-Ramirez, I., Konada, L., et al.; Mol. Cell 82, 3794 (2022), Abstract
- NLRP3 phosphorylation in its LRR domain critically regulates inflammasome assembly: T. Niu, et al.; Nat. Commun. 12, 5862 (2021), Abstract
- Ca2+/Calmodulin Binding to STIM1 Hydrophobic Residues Facilitates Slow Ca2+-Dependent Inactivation of the Orai1 Channel: Bhardwaj, R., Augustynek, B. S., et al.; Cell. Physiol. Biochem. 54, 252 (2020), Abstract
- Paxillin-Mediated Recruitment of Calcineurin to the Contractile Ring Is Required for the Correct Progression of Cytokinesis in Fission Yeast: R. Martin-Garcia, et al.; Cell Rep. 25, 772 (2018), Abstract
- Correction: A model for regulation by SynGAP-α1 of binding of synaptic proteins to PDZ-domain ‘Slots’ in the postsynaptic density: W.G. Walkup, et al.; Elife 5, e22495 (2016), Application(s): Measurement of affinity of CaM for r-synGAP-a1 by SPR, Abstract — Full Text
- The phosphatase calcineurin regulates pathological TDP-43 phosphorylation: N.F. Liachko, et al.; Acta Neuropathol. 4, 545 (2016), Abstract
- A model for regulation by SynGAP-α1 of binding of synaptic proteins to PDZ-domain ‘Slots’ in the postsynaptic density: Walkup, W. G., Mastro, T. L., et al.; Elife 5, (2016), Abstract
- Binding of synGAP to PDZ Domains of PSD-95 is Regulated by Phosphorylation and Shapes the Composition of the Postsynaptic Density: Walkup, W. G., Mastro, T., et al.; bioRxiv , (2016)
- Dissecting cooperative communications in a protein with a high-throughput single-molecule scalpel: Z. Yu, et al.; Chemphyschem. 16, 223 (2015), Abstract
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