GeneTex
United States (US)

CaMKI gamma (Active) recombinant protein

Cat No. GTX65435

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

Application Note

151 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 )
PROPERTIES

Form

Liquid

Buffer

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

Storage

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

Concentration

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

Antigen Species

Human

Expression System

Baculovirus (Sf9 insect cells)

Purification


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

Note

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

Synonyms

Calcium/Calmodulin Dependent Protein Kinase Ig,Click3,Clickiii,Vws1,Dj272L16.1,Camk1G

Background

CLICK-III/CaMKIG is a novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase (CaMK), an isoform of the CaMKI family with an extended C-terminal domain ending with CAAX motif (where AA is aliphatic acid). As expected from the similarity of its kinase domain with the other CaMKI isoforms, full activation of CLICK-III/CaMKIG required both Ca(2+)/CaM and phosphorylation by CaMKK. Ca(2+)/cAMP-response element-binding protein (CREB) was a good substrate for CLICK-III/CaMKIG, at least in vitro. Interestingly enough, CLICK-III/CaMKIG transcripts were most abundant in neurons, with the highest levels in limited nuclei such as the central nucleus of the amygdala (CeA) and the ventromedial hypothalamus. Consistent with the presence of the CAAX motif, CLICK-III/CaMKIG was found to be anchored to various membrane compartments, especially to Golgi and plasma membranes. Both point mutation in the CAAX motif and treatment with compactin, a HMG-CoA reductase inhibitor, disrupted such membrane localization, suggesting that membrane localization of CLICK-III/CaMKIG occurred in a prenylation-dependent way. These findings provide a novel mechanism by which neuronal CaMK activity could be targeted to specific membrane compartments.

Research Area

Package List Price ($)
$ 349