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anti-Human CABP1 Anticorps:
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Human Polyclonal CABP1 Primary Antibody pour ELISA, WB - ABIN249625
Yamaguchi, Yamaguchi, Miyamoto, Sugimoto, Konishi, Hatase, Tokuda: Calbrain, a novel two EF-hand calcium-binding protein that suppresses Ca2+/calmodulin-dependent protein kinase II activity in the brain. dans The Journal of biological chemistry 1999
the faster migrating Tg adduct C primarily engages the CaBP1/P5 oxidoreductase, whereas the slower migrating Tg adduct A primarily engages ERp72.
Present the NMR structure of full-length CaBP1 with Ca(2+) bound at the first, third, and fourth EF-hands.
Different kinetics of Ca-dependent binding step between caldendrin and calmodulin with AKAP79 suggest their different roles in synaptic function.
We demonstrate that calmodulin and caldendrin compete for a partially overlapping binding site on AKAP79 and that their binding is differentially dependent on calcium
CaBP1 regulates voltage-dependent inactivation and activation of Ca(V)1.2 (L-type) calcium channels
Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation.
enhances inactivation, causes a depolarizing shift in the voltage dependence of activation, and does not support Ca2+-dependent facilitation of Ca(v)2.1 channels
CaBP1 is able to specifically regulate InsP3 receptor-mediated alterations in [Ca2+]i during agonist stimulation.
We describe a new role for CaBP1 in regulation of Ca2+ influx through Ca(v)1.2 (L-type) Ca2+ channels. CaBP1 interacts directly with the alpha1 subunit of Ca(v)1.2 at sites that also bind Calmodulin
the NT and IQ-domains of alpha(1)1.2 mediate functionally distinct interactions with CaBP1 and CaM that promote conformational alterations that either stabilize or inhibit inactivation of Ca(v)1.2.
NMR, microcalorimetry, and other biophysical studies that characterize Ca(2+) binding, Mg(2+) binding, and structural properties of recombinant CaBP1 are reported.
the importance of CaBP1s in modulating the stimulus-secretion coupling in excitable cells.
CaBP1 may regulate Ca2+-dependent activity of inositol 1,4,5-trisphosphate receptors by promoting structural contacts between the suppressor and core domains
Results show that CaBP1/caldendrin and CaBP2 are not required for normal gross retinal and synapse morphology but are necessary for the proper transmission of light responses through the retina; CaBP1/caldendrin and CaBP2 likely act by modulating presynaptic Ca(2+)-dependent signaling mechanisms.
Study provides the first report of the expression and localization of CaBP1 and caldendrin in the mouse brain
our results implicate CaBP1 rather than CaBP4 in conferring the anomalous slow inactivation of Ca(v)1.3 Ca(2+) currents required for auditory transmission
Calcium binding proteins are an important component of calcium mediated cellular signal transduction. This gene encodes a protein that belongs to a subfamily of calcium binding proteins which share similarity to calmodulin. The protein encoded by this gene regulates the gating of voltage-gated calcium ion channels. This protein inhibits calcium-dependent inactivation and supports calcium-dependent facilitation of ion channels containing voltage-dependent L-type calcium channel subunit alpha-1C. This protein also regulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors, P/Q-type voltage-gated calcium channels, and transient receptor potential channel TRPC5. This gene is predominantly expressed in retina and brain. Alternative splicing results in multiple transcript variants encoding disinct isoforms.
calcium binding protein 5
, calcium-binding protein 1
, calcium binding protein 1 (calbrain)
, calcium binding protein 1