United States (US)

CaMKI delta (Active) recombinant protein

Cat No. GTX65290

Application ELISA, Functional Assay, Apuri, Blocking
Reactivity Human
Species Human

Application Note

138 nmol phosphate incorporated into Autocamtide 2 per minute per mg protein at 30ºC for 15 minutes using a final concentration of 50 uM ATP (0.83 uCi/assay).

Calculated MW

60.0 kDa. ( Note )




50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol


Store at -80ºC. Product is stable for at least 6-12 months.


0.1mg/ml(Please refer to the vial label for the specific concentration.)

Antigen Species


Expression System

Baculovirus (Sf9 insect cells)


Purity was assessed by SDS-PAGE (≥90%) and by HPLC.


For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.


Calcium/calmodulindependent protein kinase type I delta chain, CAMK, CAMK1d, Calcium/calmodulin-dependent protein kinase type I delta chain


Calcium/calmodulin-dependent protein kinase ID (CAMK1D), or a novel Ca2+/calmodulin-dependent kinase I-like kinase (CKLiK), showed kinase activity and that the activity was enhanced by Ca(2+) and calmodulin. Using a novel antibody generated against the C-terminus of CKLiK, CKLiK was detected in CD34+-derived neutrophils and eosinophils, as well as in mature peripheral blood granulocytes. Activation of human granulocytes by N-formyl-methionyl-leucyl-phenylalanine (fMLP) and platelet-activating factor (PAF), but not the phorbol ester PMA (phorbol 12-myristate-13-acetate), resulted in induction of CKLiK activity, in parallel with a rise of intracellular [Ca2+]. Furthermore, fMLP-induced neutrophil migration on albumin-coated surfaces was perturbed, as well as beta2-integrin-mediated adhesion. These findings suggest a critical role for CKLiK in modulating chemoattractant-induced functional responses in human granulocytes (1). Also, CAMK1D exhibits Ca(2+)/CaM-dependent activity that is enhanced (approximately 30-fold) in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha , consistent with detection of CAMK1D-activating activity in HeLa cells. Transiently expressed CAMK1D exhibited enhanced protein kinase activity in HeLa cells without ionomycin stimulation. This sustained activation of CAMK1D was completely abolished by Thr180Ala mutation and inhibited by CaM-KK inhibitor, STO-609, indicating a functional CaM-KK/ CAMK1D cascade in HeLa cells.

Research Area