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Human FKBP1A Protein expressed in Wheat germ - ABIN1354116
Åström-Olsson, Li, Olofsson, Borén, Öhlin, Grip: Impact of hypoxia, simulated ischemia and reperfusion in HL-1 cells on the expression of FKBP12/FKBP12.6 and intracellular calcium dynamics. in Biochemical and biophysical research communications 2012
Show all 3 Pubmed References
Acute tacrolimus treatment transiently increases hepcidin (show HAMP Proteins) in wild-type mice. FKBP12 preferentially targets the BMP receptor (show BMPR1A Proteins) ALK2 (show ACRV1 Proteins). ALK2 (show ACRV1 Proteins) mutants defective in binding FKBP12 increase hepcidin (show HAMP Proteins) expression in a ligand-independent manner, through BMP-SMAD (show SMAD1 Proteins) signaling.
FKBP51 (show FKBP5 Proteins) is a central mediator of chronic pain.
We demonstrate that FKBP12 and its ligands impact multiple aspects of muscle function.
Fkbp1a-mediated regulation of Notch1 (show NOTCH1 Proteins) plays an important role in intercellular communication between endocardium and myocardium.
FKBP12 is critically important in regulating trans-sarcolemmal ionic currents, predominately the voltage-gated Na+ current, I Na
the impact of simulated ischemia and reperfusion on expression of the calcium handling proteins FKBP12 and FKBP12.6 (show FKBP1B Proteins), and intracellular calcium dynamics was investigated.
Data show that deletion of FKBP12 increased transforming growth factor-beta receptor activation and SMAD2 (show SMAD2 Proteins)/3 signaling.
FKBP12 is a critical regulator of I(Na) and is important for cardiac arrhythmogenic physiology
a trimeric-interaction among calcineurin, FKBP12, and RyR (show RYR1 Proteins) is important for the regulation of the RyR (show RYR1 Proteins) channel activity and may play an important role in the Ca(2 (show CA2 Proteins)+) signaling of muscle contraction and relaxation
FKBP12 binding to RyR1 (show RYR1 Proteins) enhances the gain of skeletal muscle excitation-contraction coupling
Data indicate that S107 increased FKBP12 binding to RyR1 (show RYR1 Proteins) in sarcoplasmic reticulum vesicles in the presence of reduced glutathione and the NO-donor NOC12.
A mutant with substitution at the sole cysteine residue of FKBP-12 (C23S) did not form dimers or trimers.
phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding.
expression higher in the silk gland and gut (show GUSB Proteins)
A cDNA encoding the 12 kDa FKBP gene orthologue (FKBP12) in Bombyx mori was been isolated from both Bm-5 cultured cells and silk-gland tissue.
These findings of this study suggested that FKBP12 is linked to the accumulation of alpha-SYN and phosphorylated tau protein in alpha-synucleinopathies. FKBP12 may play important roles in the pathogenesis of alpha-synucleinopathies.
ubiquitylation destabilizes the fold of two proteins, FKBP12 and FABP4 (show FABP4 Proteins)
FKBP12 binding is required for full Met activation and everolimus can inhibit Met
Specifically tested on two model systems, the power of iSPOT is demonstrated to accurately predict the structures of a large protein-protein complex (TGFbeta (show TGFB1 Proteins)-FKBP12) and a multidomain nuclear receptor homodimer (HNF-4alpha (show HNF4A Proteins)), based on the structures of individual components of the complexes.
These results identify a novel function for FKBP12 in downregulating MDM2 (show MDM2 Proteins), which directly enhances sensitivity of cancer cells to chemotherapy and nutlin-3 treatment.
Data show that FKBP12 (FK506 binding protein 1A)conformational transition Is coupled to histidine tautomerization.
Electrostatic effects on the folding stability of FKBP12
Findings indicate that mutant huntingtin (mHTT) aggregates can be transformed into benign species by isomerase FKBP12.
RyRs have been identified as important targets of FKBP12 and FKBP12.6 (show FKBP1B Proteins), members of the immunophilin family
How phosphorylation of RyR (show RYR1 Proteins) affects channel activity and whether proteins such as the FK-506 binding proteins (FKBP12 and FKBP12.6 (show FKBP1B Proteins)) are involved in heart failure
Stoichiometry of binding sites and FKBP (show FKBP7 Proteins) 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. The protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels, and coordinates multi-protein complex formation of the tetrameric skeletal muscle ryanodine receptor. In mouse, deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium. Multiple alternatively spliced variants, encoding the same protein, have been identified. The human genome contains five pseudogenes related to this gene, at least one of which is transcribed.
12 kDa FK506-binding protein
, 12 kDa FKBP
, FK506 Binding Protein12-T1
, FK506 binding protein12
, FK506 binding protein12-T2
, FK506-binding protein 1A
, PPIase FKBP1A
, immunophilin FKBP12
, peptidyl-prolyl cis-trans isomerase FKBP1A
, Immunophilin FKBP12
, binding protein
, FK506-binding protein
, FK506-binding protein 1
, FK506-binding protein 12
, FK506-binding protein 1A (12kD)
, FK506-binding protein, T-cell, 12-kD
, calstabin 1
, protein kinase C inhibitor 2
, FK506 binding protein 1B, 12.6 kDa
, FK506 binding protein 2 (13 kDa)
, FK506-binding protein 1 (12kD)
, FK506-binding protein 1a
, FK506 binding protein 1A, 12kDa
, fk506-binding protein
, FK506-binding protein-like
, FK 506-binding protein