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The protein encoded by CACNB1 belongs to the calcium channel beta subunit family. Additionally we are shipping CACNB1 Proteins (7) and many more products for this protein.
Showing 10 out of 114 products:
Human Polyclonal CACNB1 Primary Antibody for EIA, WB - ABIN950992
Jangsangthong, Kuzmenkina, Khan, Matthes, Hullin, Herzig: Inactivation of L-type calcium channels is determined by the length of the N terminus of mutant beta(1) subunits. in Pflügers Archiv : European journal of physiology 2010
Show all 3 references for ABIN950992
Human Polyclonal CACNB1 Primary Antibody for WB - ABIN265036
Collin, Wang, Nargeot, Schwartz: Molecular cloning of three isoforms of the L-type voltage-dependent calcium channel beta subunit from normal human heart. in Circulation research 1993
Show all 2 references for ABIN265036
Human Monoclonal CACNB1 Primary Antibody for ICC, IF - ABIN361776
Leyris, Gondeau, Charnet, Delattre, Rousset, Cens, Charnet: RGK GTPase-dependent CaV2.1 Ca2+ channel inhibition is independent of CaVbeta-subunit-induced current potentiation. in The FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2009
Human Monoclonal CACNB1 Primary Antibody for RNAi, ELISA - ABIN560140
Zou, Jha, Kim, Dryer: The beta 1 subunit of L-type voltage-gated Ca2+ channels independently binds to and inhibits the gating of large-conductance Ca2+-activated K+ channels. in Molecular pharmacology 2008
Chicken Polyclonal CACNB1 Primary Antibody for WB - ABIN2776354
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
Cow (Bovine) Polyclonal CACNB1 Primary Antibody for WB - ABIN2776092
Hogan, Greg, Powers: Structure and alternative splicing of the gene encoding the human beta1 subunit of voltage dependent calcium channels. in Neuroscience letters 2000
Cow (Bovine) Polyclonal CACNB1 Primary Antibody for IHC, WB - ABIN2776353
Foell, Balijepalli, Delisle, Yunker, Robia, Walker, McEnery, January, Kamp: Molecular heterogeneity of calcium channel beta-subunits in canine and human heart: evidence for differential subcellular localization. in Physiological genomics 2004
beta subunits, probably via the SH3-C-terminal polyproline interaction, adapt a discrete conformation required to modify the alpha1S conformation apt for voltage sensing in skeletal muscle.
Disruption of functional dihydropyridine receptor (show CACNA1S Antibodies) (DHPR (show QDPR Antibodies))-ryanodine receptor (show RYR3 Antibodies) (RyR1 (show RYR1 Antibodies)) interactions caused by lack of the beta 1a subunit is responsible for paralysis of skeletal muscle in beta 1-null muscle cells.
Relaxed mutant muscles are defective in excitation-contraction coupling. The mutant phenotype results from non-sense mutations in the zebrafish CACNB1 gene that encodes the DHPR (show QDPR Antibodies) beta1 subunit.
triad expression and facilitation of 1,4-dihydropyridine receptor (show CACNA1S Antibodies) (DHPR (show QDPR Antibodies)) charge movement are common features of all tested beta subunits
These results provide new insights into the role of muscle-specific (show EIF3K Antibodies) proteins on the structural arrangement of alpha1S intracellular loops and point to a new conformational effect of the beta1a subunit in supporting skeletal muscle excitation-contraction coupling.
CACNB1, encoding cardiac L-type calcium channel beta 1 subunit, is a potential target for microRNA-328 in transgenic mice.
The present study reveals that the C-terminal of the beta1a subunit changes conformation in the presence of RyR1 (show RYR1 Antibodies) consistent with an interaction between the C-terminal of beta1a and RyR1 (show RYR1 Antibodies) in resting myotubes.
The motif Leu(496)-Leu(500)-Trp (show TYRP1 Antibodies)(503) within the bet1a C-terminal tail plays a nonessential role in the bidirectional DHPR (show QDPR Antibodies)/RyR1 (show RYR1 Antibodies) signaling that supports skeletal-type excitation-contraction coupling.
Cavbeta1a acts as a Cav (show CA5A Antibodies)-independent regulator of gene expression in MPCs, and is required for their normal expansion during myogenic development.
Data suggest that specific hydrophobic surface residues in calcium channel voltage-dependent beta1a subunit C-terminus bind to RyR1 (show RYR1 Antibodies) and increase channel activity in lipid bilayers and thus may support skeletal muscle excitation-contraction coupling.
The results of this study indicated that the skeletal muscle DHPR (show QDPR Antibodies) retrogradely regulates the patterning and formation of the Neuromuscular junction.
Mice with cardiac-specific sequestration of the beta-subunit (show POLG Antibodies) of the L-type calcium channel
calcium channel beta1a subunits are organized in triad junctions in skeletal muscle
excitation-contraction coupling in skeletal muscle involves the interplay of at least two subunits of the DHPR (show QDPR Antibodies), namely alpha1S and beta1a, interacting with possibly different domains of RyR1 (show RYR1 Antibodies) [DHPR (show QDPR Antibodies) beta1a]
absence of alpha1S, beta1 or gamma1 DHPR (show QDPR Antibodies) subunits does not significantly affect the electrophysiological properties of T-type Ca2 (show CA2 Antibodies)+ currents in skeletal muscle
The protein encoded by this gene belongs to the calcium channel beta subunit family. It plays an important role in the calcium channel by modulating G protein inhibition, increasing peak calcium current, controlling the alpha-1 subunit membrane targeting and shifting the voltage dependence of activation and inactivation. Alternative splicing occurs at this locus and three transcript variants encoding three distinct isoforms have been identified.
calcium channel, voltage-dependent, beta 1 subunit
, voltage-dependent L-type calcium channel subunit beta-1-like
, calcium channel beta1a subunit
, dihydropyridine receptor b1
, dihydropyridine receptor beta 1a subunit
, dihydropyridine receptor beta 1c subunit
, voltage-dependent L-type calcium channel subunit beta-1
, calcium channel voltage-dependent subunit beta 1
, calcium channel, L type, beta 1 polypeptide
, dihydropyridine-sensitive L-type, calcium channel beta-1 subunit
, voltage dependent calcium channel, beta1 subunit, variant5
, voltage-dependent calcium channel beta1 subunit
, brain calcium channel beta 1 subunit
, calcium channel beta 1 subunit