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The protein encoded by FKBP10 belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. Additionally we are shipping FK506 Binding Protein 10, 65 KDa Antibodies (62) and FK506 Binding Protein 10, 65 KDa Kits (1) and many more products for this protein.
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Data suggest a requirement for FKBP65 function during embryonic connective tissue development in mice; its expression is restricted postnatally in bone, ligaments and tendons.
FKBP65 may act as an elastin (show ELN Proteins) chaperone in vivo by controlling both the coacervation and the maturation stages of its selfassembly into fibrils.
FKBP10 protein is overexpressed in renal cell carcinoma (show MOK Proteins)
FKBP65 is linked to pyridinoline cross-linking by specifically mediating the dimerization of LH2 (show PLOD2 Proteins).
observed changes in activity of six rER-resident PPIases, cyclophilin B (show PPIB Proteins) (encoded by the PPIB (show PPIB Proteins) gene), FKBP13 (FKBP2 (show FKBP2 Proteins)), FKBP19 (FKBP11 (show FKBP11 Proteins)), FKBP22 (FKBP14 (show FKBP14 Proteins)), FKBP23 (FKBP7 (show FKBP7 Proteins)), and FKBP65 (FKBP10), due to posttranslational modifications of proline residues in the substrate.
novel pathogenic mutations of FKBP10 can lead to the extremely rare type XI Osteogenesis imperfecta (show COL1A2 Proteins) without contractures, which expands the genotypic spectrum of Osteogenesis imperfecta (show COL1A2 Proteins).
Mutations in FKBP10, localised to chromosome 17q21, have been identified in a patient of Bruck syndrome. Additional cases are also discussed.
A pathogenic change was found in the FKBP10 gene in patients with osteogenesis imperfecta (show COL1A2 Proteins).
findings further extend the body of evidence that supports the importance of FKBP10 gene in the development of skeletal system
Mutations in the HSP47 and FKBP65 produce a moderately severe form of Osteogenesis imperfect.
CTSD (show CTSD Proteins), FKBP10, and SLC2A1 (show SLC2A1 Proteins) are novel genes that participate in the acquisition and maintenance of the adriamycin-resistant phenotype in leukemia cells.
Results imply that FKBP10 mutations affect collagen indirectly, by ablating FKBP65 support for collagen telopeptide hydroxylation by lysyl hydroxylase 2 (show PLOD2 Proteins), thus decreasing collagen cross-links in tendon and bone matrix.
The protein encoded by this gene belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. This protein localizes to the endoplasmic reticulum and acts as a molecular chaperone. Alternatively spliced variants encoding different isoforms have been reported, but their biological validity has not been determined.
FK506 binding protein 10
, FK506 binding protein 10, 65 kDa
, peptidyl-prolyl cis-trans isomerase FKBP10
, FK506-binding protein
, peptidyl-prolyl cis-trans isomerase FKBP10-like
, 65 kDa FK506-binding protein
, 65 kDa FKBP
, FK506 binding protein 6 (65 kDa)
, FK506-binding protein 10
, PPIase FKBP10
, immunophilin FKBP65