form
saline suspension
extent of labeling
≥0.5 mg per mL
matrix
4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
storage temp.
2-8°C
Application
Calmodulin-agarose is used in affinity chromatography, protein chromatography, calcium associated proteins, and specialty resins. Calmodulin-agarose has been used to suggest a coordinated regulation of processes in both mitochondria and chloroplasts by calcium signals. Calmodulin-agarose has also been used to study apoptosis in prostate cancer cells and to analyze the interaction of the influenza virus polymerase complex with human cell factors.
Physical form
Suspension in 0.5 M NaCl containing 0.02% thimerosal
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
S J Lee et al.
Neuron, 32(6), 1097-1106 (2002-01-05)
Hundreds of G protein-coupled receptors (GPCRs) and at least six GPCR kinases have been identified, but the only GPCR phosphatase that has been definitively demonstrated is the rhodopsin phosphatase encoded by the rdgC locus of Drosophila. Mutations in rdgC result
J A Porter et al.
Science (New York, N.Y.), 262(5136), 1038-1042 (1993-11-12)
Calmodulin is a highly conserved regulatory protein found in all eukaryotic organisms which mediates a variety of calcium ion-dependent signalling pathways. In the Drosophila retina, calmodulin was concentrated in the photoreceptor cell microvillar structure, the rhabdomere, and was found in
Danton H O'Day et al.
Biochemical and biophysical research communications, 331(4), 1494-1502 (2005-05-11)
Probing of a cDNA expression library from multicellular development of Dictyostelium discoideum using a recombinant radiolabelled calmodulin probe (35S-VU1-CaM) led to the isolation of a cDNA encoding a putative CaM-binding protein (CaMBP). The cDNA contained an open reading frame of
A Schwarzer et al.
The Journal of biological chemistry, 275(18), 13448-13454 (2000-05-02)
The intracellular Ca(2+) concentration in rod outer segments of vertebrate photoreceptors is controlled by Ca(2+) influx through cGMP-gated channels and by Ca(2+) efflux driven by Na/Ca-K exchangers. Previously, we suggested that channel and exchanger are associated (Bauer, P. J., and
A Takasaki et al.
The Journal of biological chemistry, 274(17), 11848-11853 (1999-04-17)
Various proteins in the signal transduction pathways as well as those of viral origin have been shown to be myristoylated. Although the modification is often essential for the proper functioning of the modified protein, the mechanism by which the modification
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