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Human Polyclonal FKBP14 Primary Antibody pour WB - ABIN527313
Baumann, Giunta, Krabichler, Rüschendorf, Zoppi, Colombi, Bittner, Quijano-Roy, Muntoni, Cirak, Schreiber, Zou, Hu, Romero, Carlier, Amberger, Deutschmann, Straub, Rohrbach, Steinmann, Rostásy et al.: Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss. ... dans American journal of human genetics 2012
FKBP14 may act as an oncogene through suppressing apoptosis and promoting motility in human cervical carcinogenesis.
Genetic studies showed that the patient harboured a homozygous mutation (c.362dupC p.Glu122Argfs*7) in the FKBP14 gene, confirming kyphoscoliotic EDS related to this gene.
FKBP14 may act as an oncogene in osteosarcoma via suppressing apoptosis and promoting invasion and adhesion in osteosarcoma carcinogenesis
this report describes a potentially life-threatening vascular complication in early pediatric age and atlantoaxial instability, suggesting the need for FKBP14-related EDS patients of tailored follow-up that includes cardiovascular monitoring, that is, cerebral, thoracic and abdominal MRA, and cervical dynamic radiograph.
observed changes in activity of six rER-resident PPIases, cyclophilin B (encoded by the PPIB gene), FKBP13 (FKBP2), FKBP19 (FKBP11), FKBP22 (FKBP14), FKBP23 (FKBP7), and FKBP65 (FKBP10), due to posttranslational modifications of proline residues in the substrate.
FKBP14 expression was elevated in ovarian cancer tissues when compared with matched normal tissues. Lentiviral shRNA mediated knockdown of FKBP14 and suppressed the growth of ovarian cancer cells via arresting the cell cycle in the G0/G1 phase and stimulating cell apoptosis. Moreover, cell apoptosis induced by FKBP14 RNAi was mediated by enhancing the ratio of Bax/Bcl-2.
Reduced expression of FKBP14 markedly impaired the proliferative ability of ovarian cancer cells. Additionally, ovarian cancer cells infected with FKBP14 shRNA lentivirus tended to arrest in the G0/G1 phase and undergo apoptosis.
the occurrence of umbilical skin redundancy in association with two other syndromes: Morquio syndrome and FKBP14-related Ehlers-Danlos syndrome (EDS), is reported.
FKBP22 catalyzes the folding of type III collagen and only interacts with type III type VI and type X collagen.
A 1.9 A resolution crystal structure for human FKBP22 has been determined. The EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand.
study demonstrated FKBP14 is localized in the endoplasmic reticulum (ER) and that deficiency of FKBP14 leads to enlarged ER cisterns in dermal fibroblasts in vivo.
The protein encoded by this gene is a member of the FK506-binding protein family of peptidyl-prolyl cis-trans isomerases. The encoded protein is found in the lumen of the endoplasmic reticulum, where it is thought to accelerate protein folding. Defects in this gene are a cause of a type of Ehlers-Danlos syndrome (EDS). Both a protein-coding variant and noncoding variants are transcribed from this gene.
FK506 binding protein 14, 22 kDa
, FK506-binding protein 14
, PPIase FKBP14
, peptidyl-prolyl cis-trans isomerase FKBP14
, 22 kDa FK506-binding protein
, 22 kDa FKBP