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anti-Mouse (Murine) FKBP1B Antibodies:
anti-Rat (Rattus) FKBP1B Antibodies:
anti-Human FKBP1B Antibodies:
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The heart contraction is controlled by the Ca2 (show CA2 Antibodies)+-induced Ca2 (show CA2 Antibodies)+ release between L-type Ca2 (show CA2 Antibodies)+ channels and ryanodine receptors. RyRs became more sensitive to Ca2 (show CA2 Antibodies)+ triggers without FKBP12.6, leading to ventricular arrthymias.
Calstabin2 as a key modulator of cardiac aging.
Sirolimus-FKBP12.6 impairs endothelial barrier function by activation of protein kinase C-alpha (show PKCa Antibodies) and downstream disruption of the p120 (show CTNND1 Antibodies)-VE cadherin (show CDH5 Antibodies) interaction in vascular endothelium.
genetic approaches confirm the role of FKBP12.6 in regulating cardiac ryanodine receptors
the impact of simulated ischemia and reperfusion on expression of the calcium handling proteins FKBP12 (show FKBP1A Antibodies) and FKBP12.6, and intracellular calcium dynamics was investigated.
Transcription factor CHF1/Hey2 (show HEY2 Antibodies) regulates EC coupling and heart failure in mice through regulation of FKBP12.6.
Cardiac FKBP12.6 overexpression in the mouse blunts pressure overload-induced maladaptive left ventricular remodelling.
FKBP12.6 removal enhanced, whereas RyR2 (show RYR2 Antibodies) gene deletion blocked the hypoxic increase in Ca(2 (show CA2 Antibodies)+)(i) in pulmonary artery smooth muscle cells.
Characterize the kinetics of FKBP12 (show FKBP1A Antibodies)/12.6 binding to RyR2 (show RYR2 Antibodies) in ventricular myocytes and effects on calcium signaling.
FKBP12.6(-/-) mice displayed hyperinsulinemia, & resistance to high fat diet-induced hyperglycemia, suggesting that FKBP12.6 plays an important role in insulin (show INS Antibodies) secretion & blood glucose control.
Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin (show FKBP1A Antibodies) calstabin 2
results suggest that both FKBP12.6 and FKBP12 play critical roles in regulating RyR2 (show RYR2 Antibodies) function by facilitating the termination of SOICR.
RyRs have been identified as important targets of FKBP12 and FKBP12.6, members of the immunophilin (show FKBP1A Antibodies) family
How phosphorylation of RyR (show RYR1 Antibodies) affects channel activity and whether proteins such as the FK-506 binding proteins (FKBP12 and FKBP12.6) are involved in heart failure
Sirolimus-FKBP12.6 impairs endothelial barrier function by activation of protein kinase C-alpha (show PKCa Antibodies) and downstream disruption of the p120 (show HNRNPU Antibodies)-VE cadherin (show CDH5 Antibodies) interaction in vascular endothelium.
These data corroborate other studies suggesting that mutations in FKBP12 and FKBP12.6 genes are not commonly related to cardiac diseases.
FKBP12.6-deficient mice with cardiac hypertrophy do not display exercise-induced arrhythmia and/or sudden cardiac death.
analysis of the ryanodine receptor (show RYR3 Antibodies) FK506-binding protein (show FKBPL Antibodies) subunit
Characterize the kinetics of FKBP12/12.6 binding to RyR2 (show RYR2 Antibodies) in ventricular myocytes and effects on calcium signaling.
localization of binding site to the NH2-terminal domain of the cardiac Ca2+ release channel (show RYR2 Antibodies)
Study determined the three-dimensional structure of rabbit RyR2 (show RYR2 Antibodies) in complex with the regulatory protein FKBP12.6 in the closed state at 11.8 A resolution using cryo-electron microscopy and built an atomic model of RyR2 (show RYR2 Antibodies).
phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding.
Stoichiometry of binding sites and FKBP (show FKBP7 Antibodies) exchange binding.
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.
FK506 binding protein 12.6
, peptidyl-prolyl cis-trans isomerase FKBP1B
, FK506 binding protein 1B, 12.6 kDa
, 12.6 kDa FK506-binding protein
, 12.6 kDa FKBP
, FK506-binding protein 12.6
, FK506-binding protein 1B
, PPIase FKBP1B
, immunophilin FKBP12.6
, calstabin 2
, Immunophilin FKBP12.6
, PPIase 1B
, Rotamase 1B
, peptidyl-prolyl cis-trans isomerase 1B
, peptidyl-prolyl cis-trans isomerase; PPIase