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Human Monoclonal FKBP4 Primary Antibody pour IHC (p), IP - ABIN560907
Desmetz, Bascoul-Mollevi, Rochaix, Lamy, Kramar, Rouanet, Maudelonde, Mangé, Solassol: Identification of a new panel of serum autoantibodies associated with the presence of in situ carcinoma of the breast in younger women. dans Clinical cancer research : an official journal of the American Association for Cancer Research 2009
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Human Monoclonal FKBP4 Primary Antibody pour ELISA, WB - ABIN535231
Ma, Bai, Guo, Jiang: The switch I region of Rheb is critical for its interaction with FKBP38. dans The Journal of biological chemistry 2008
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Human Polyclonal FKBP4 Primary Antibody pour ELISA, WB - ABIN449657
Ruan, Pong, Jow, Bowlby, Crozier, Liu, Liang, Chen, Mercado, Feng, Bennett, von Schack, McDonald, Zaleska, Wood, Reinhart, Magolda, Skotnicki, Pangalos, Koehn, Carter, Abou-Gharbia, Graziani: Binding of rapamycin analogs to calcium channels and FKBP52 contributes to their neuroprotective activities. dans Proceedings of the National Academy of Sciences of the United States of America 2008
Human Polyclonal FKBP4 Primary Antibody pour ICC, IF - ABIN261152
Rho, Lampe: High-throughput screening for native autoantigen-autoantibody complexes using antibody microarrays. dans Journal of proteome research 2013
Human Polyclonal FKBP4 Primary Antibody pour ICC, IF - ABIN4312026
Tyleckova, Hrabakova, Mairychova, Halada, Radova, Dzubak, Hajduch, Gadher, Kovarova: Cancer cell response to anthracyclines effects: mysteries of the hidden proteins associated with these drugs. dans International journal of molecular sciences 2013
Study demonstrates that FKBP52 by itself does not directly affect cognition and may play an indirect, modulatory role in the functional pathology of Alzheimer's disease, whereas it directly affects motor coordination, an early sign of neurodegenerative damages to the brain.
identify a novel steroid-responsive FKBP52-dependent pathway suppressing the expression and activity of tryptophan-2,3-dioxygenase
study identifies Fkbp4 and Fkbp5 as novel components of the Ago2 RISC loading complex
FKBP52 is not involved in all branches of GR signaling, but rather acts in a gene-specific manner to regulate GR transcriptional activation.
FKBP52 regulates androgen receptor function through the BF3 surface.
Findings suggest that Fkbp52 deficiency diminishes the threshold against OS by reducing PRDX6 levels.
Fkbp52 is an important molecular regulator in the androgen-mediated pathway of urethra morphogenesis.
Data propose a model in which FKBP52 loss reduces GR control of gluconeogenesis, predisposing the liver to steatosis under HF-diet conditions attributable to a shunting of metabolism from glucose production to lipogenesis.
a Hoxa10-FKBP52 signaling axis is critical to uterine receptivity and implantation
FKBP52 is an AR folding factor that has critically important physiological roles in some male reproductive tissues
Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation.
Fkbp52 but not Fkbp51 is essential to androgen receptor mediated signaling
indispensability of FKBP52 in uterine progesterone/progesterone receptor signaling is a function of genetic disparity and is pregnancy stage specific
phosphorylation of the FK linker appears to be an important regulatory determinant of FKBP52-mediated potentiation of steroid receptor activity
These results suggest that the FK1 domain, and in particular the loop overhanging the catalytic pocket, is critically involved in receptor interactions and receptor activity.
Data show that the loss of FKBP52 encourages the growth of endometriotic lesions with increased inflammation, cell proliferation, and angiogenesis.
FKBP52 does not contribute to all branches of GR signaling.
elevated FKBP4 expression was associated with poor survival of patients with hormone-naive prostate cancer
ID4 selectively regulates AR activity through direct interaction with FKBP52.
FKBP52 could be abnormally released from NFTs negative neurons in AD brains in correlation with the early pathologic Tau-D(421) neuronal accumulation.
Mechanistically, USP49 deubiquitinates and stabilizes FKBP51, which in turn enhances PHLPP's capability to dephosphorylate AKT.
Low expression of FKBP4 is associated with Progesterone Resistance in Endometriosis.
Results provide a molecular mechanism by which FKBP52 modulates telomerase activity by promoting dynein-dynactin-dependent nuclear import of hTERT.
The Hsp90-associated FKBP52 cochaperone has become increasingly associated with aberrant steroid hormone receptor signaling in disease. [review]
The capacity FKBP52 to oligomerize Tau is not linked to its peptidyl-prolyl isomerase activity.
FKBP52 and beta-catenin interact directly in vitro. FKBP52 promotes beta-catenin interaction with androgen receptor signaling.
FKBP4 was not differentially expressed in PTSD patients with low HPA axis reactivity compared to PTSD patients with high HPA axis reactivity.
FKBP51 is the major target accounting for the neuritotrophic effect of neuroimmunophilin ligands. Selectivity against the homolog FKBP52 is essential for optimal neuritotrophic efficacy.
FKBP52 seems to be disrupted in preeclampsia and intrauterine growth restriction pregnancies
The biological action of NF-kappaB in different cell types could be positively regulated by a high FKBP52/FKBP51 expression ratio.
Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52
Despite their substantial structural similarity, in both the beta3 bulge and the beta4-beta5 loop, the FK1 domain of FKBP51 undergoes significantly populated conformational transitions that appear to be suppressed in FKBP52.
FKBP52 appears to be an endogenous candidate that directly interacts with the pathogenic Tau-P301L and modulates its function in vitro and in vivo
The guinea pig GR-specific mutations within the H1-H3 loop confer global changes within the GR-Hsp90 complex that favor FKBP51 repression over FKBP52 potentiation.
FKBP4, p23, and Aha1 cooperatively regulate the progression of hAgo2 through the chaperone cycle.
This study does not confirm a role for genetic variants in the SFRS3 and FKBP4 genes in the pathogenesis of corticosteroid-induced ocular hypertension.
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 to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. The human genome contains several non-transcribed pseudogenes similar to this gene.
peptidyl-prolyl cis-trans isomerase FKBP4
, FK506-binding protein 4
, FK506 binding protein 4, 59kDa
, peptidyl-prolyl cis-trans isomerase FKBP4-like
, 52 kDa FK506-binding protein
, 52 kDa FKBP
, 59 kDa immunophilin
, HSP-binding immunophilin
, PPIase FKBP4
, immunophilin FKBP52
, FK506 binding protein 52
, FKBP52 protein
, 51 kDa FK506-binding protein
, FK506-binding protein 4 (59kD)
, HSP binding immunophilin
, T-cell FK506-binding protein, 59kD
, peptidylprolyl cis-trans isomerase
, hsp90 binding protein
, p59 protein