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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 in wild-type mice. FKBP12 preferentially targets the BMP receptor ALK2. ALK2 mutants defective in binding FKBP12 increase hepcidin expression in a ligand-independent manner, through BMP-SMAD signaling.
FKBP51 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 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, and intracellular calcium dynamics was investigated.
Data show that deletion of FKBP12 increased transforming growth factor-beta receptor activation and SMAD2/3 signaling.
FKBP12 is a critical regulator of I(Na) and is important for cardiac arrhythmogenic physiology
a trimeric-interaction among calcineurin, FKBP12, and RyR is important for the regulation of the RyR channel activity and may play an important role in the Ca(2+) signaling of muscle contraction and relaxation
FKBP12 binding to RyR1 enhances the gain of skeletal muscle excitation-contraction coupling
used systemic gene transfer in tumor-bearing mice to identify novel antiinvasive and antimetastatic functions for Fkbp8, and subsequently for Fkbp1a
FKBP12 deficiency alters both orthograde and retrograde coupling between the L-type Ca2+ channel and RyR1 and the consequences of these changes depend on muscle type and activity
manipulating the stoichiometry between calstabin2 and ryanodine receptor 2 can restore normal cardiac function in vivo
analysis of FK506-rapamycin binding (FRB) protein mutant rescue with chemical ligands
These data strongly suggests that FKBP-12 is altered in an experimental model of PD.
FKBP12 deficiency results in less initial strength deficits and enhanced recovery from single (especially females) and repeated bouts of injury than wild type mice
The results of this study indicate that FKBP12 plays a critical role in the regulation of mTOR-Raptor interactions, LTP, memory, and perseverative behaviors.
tacrolimus alters intracellular calcium and eNOS by binding to FKBP
Data indicate that S107 increased FKBP12 binding to RyR1 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
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
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-FKBP12) and a multidomain nuclear receptor homodimer (HNF-4alpha), based on the structures of individual components of the complexes.
These results identify a novel function for FKBP12 in downregulating MDM2, 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, members of the immunophilin family
How phosphorylation of RyR affects channel activity and whether proteins such as the FK-506 binding proteins (FKBP12 and FKBP12.6) are involved in heart failure
Ultra-fast Shape Recognition with Atom Types--the discovery of novel bioactive small molecular scaffolds for FKBP12 and 11betaHSD1.
Selectivity within the FKBP family, in particular selective inhibition of FKBP12 or FKBP51, is possible. FKBP51 is a pharmacologically tractable target for stress-related disorders.
peptidyl prolyl cis-trans isomerase activity of FKBP12 probably plays a role in inhibition of receptor phosphorylation.
FKBP12 inhibits RyR1 and FKBP12 E31Q/D32N/W59F mutant activates RyR1 in vitro.
FKBP12 regulates the localization and processing of amyloid precursor protein in human cell lines.
Enhanced plasticity in the active site of FKBP12.6 is likely to contribute to marked attenuation in the spatial extent of the residues that exhibit doubling of their amide resonances compared with those of the homologous FKBP12.
the structural basis of the slow resonance doubling transition of FKBP12 and the more rapid conformational linebroadening transition in the 80's loop to gain insight into how these effects are propagated through the protein structure
the association of FKBP12 with OPRM1 attenuates the phosphorylation of the receptor and triggers the recruitment and activation of PKCepsilon.
The K44V mutation selectively reduces the line-broadening in the 40's loop, verifying that at least three distinct conformational transitions underlie the line-broadening processes of FKBP12.
N-terminal and central domain elements are closely apposed near the FKBP12 binding site within the RyR1 three-dimensional structure.
Stoichiometry of binding sites and FKBP 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