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anti-Human CHM Antibodies:
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Human Polyclonal CHM Primary Antibody for WB - ABIN1881197
Renner, Fiebig, Cropp, Weber, Kellner: Progression of retinal pigment epithelial alterations during long-term follow-up in female carriers of choroideremia and report of a novel CHM mutation. in Archives of ophthalmology 2009
Horse (Equine) Polyclonal CHM Primary Antibody for WB - ABIN2792245
Ishiguro, Yamamoto, Fujita, Akasu, Kobayashi, Moriya: Effect of a clinical pathway after laparoscopic surgery for colorectal cancer. in Hepato-gastroenterology 2008
Show all 2 Pubmed References
In Choroideremia(Y42X/y) fibroblasts, there was a recovery of prenylation activity following treatment with either PTC124 (42 +/- 5%) or PTC-414 (36 +/- 11%), although an increase in REP1 protein was not detected in these cells, in contrast to the zebrafish model.
The degenerative phenotype resulting from a null mutation in the zebrafish gene indicates that hair cells and retinal cells require Rab escort protein 1 for survival.
The results of this study propose that in chm(-/-) zebrafish, maternally derived rep allows initial successful development of the embryo, but its gradual loss leads to multisystem disease and invariably to lethality.
Overexpression of REP1 in BEAS-2B cells enhanced cell growth and anchorage-independent colony formation with little increase in EGFR (show EGFR Antibodies) level and STAT3 (show STAT3 Antibodies) activation.
we demonstrated that REP1 blocked the nuclear trans-localization of FOXO3 through physically interacting with FOXO3, thereby suppressing FOXO3-mediated apoptosis. Importantly, the inhibition of REP1 combined with 5-FU treatment could lead to significant retarded tumor growth in a xenograft tumor model of human cancer cells
Our results showed CNV within the Rep-1 gene could be an important contributor in Chinese Choroideremia patients.
We describe the causative mutations in a large cohort of patients who also were examined clinically and explore potential genotype-phenotype correlations. By so doing, we further aimed to make inferences regarding the importance of particular regions of the CHM gene with respect to mutagenesis and to infer the importance of particular regions of the REP1 protein essential for normal function.
Six previously reported and five novel CHM mutations were detected in 11 Australian families clinically diagnosed with choroideremia.
The family segregated a REP1 mutation, suggesting choroideremia (CHM).
We report a novel CHM mutation, c.1475_1476insCA, identified by whole-exome sequencing in a family with X-linked CHM initially diagnosed as retinitis pigmentosa.
Sanger sequencing confirmed the mutations in CHM, including four novel (c.558_559delTT, c.964G>T, c.966delA, c.1166+2T>G) and two known (c.7031G>A and c.1584_1587delTGTT) mutations.
the clinical and molecular findings of an Italian family with a new mutation in the choroideremia (CHM) gene, are reported.
data demonstrate that SFPQ (show SFPQ Antibodies) orchestrates spatial gene expression of a newly identified RNA regulon essential for axonal viability.
These results are compatible with the idea that SFPQ (show SFPQ Antibodies), plays an important role regulating proliferation and migration during the development of the cerebral cortex.
these results show that PSF (show IL-3 Antibodies) can repress the transcriptional activation of VEGF (show VEGFA Antibodies) stimulated by IGF-1 (show IGF1 Antibodies) via recruitment of the Hakai (show CBLL1 Antibodies) complex
Quantitative proteomics reveals dynamic interaction of JNK (show MAPK8 Antibodies) with RNA transport granule proteins Sfpq (show SFPQ Antibodies) and Nono (show NONO Antibodies) during neuronal differentiation
Loss of the Chm/Rep1 gene causes premature accumulation of features of aging in the retinal pigment epithelium.
A protein complex was identified containing PSPC1 (show PSPC1 Antibodies), PSF (show IL-3 Antibodies) and LMX1B (show LMX1B Antibodies), suggesting the existence of this complex in mesodiencephalic dopaminergic neurons.
PSF (show IL-3 Antibodies) contributes to the stability of a subset of histone genes and that loss of H2AE (show HIST1H2AJ Antibodies) expression in the PSF (show IL-3 Antibodies)-deficient thymocytes uniquely contributes to an increase in thymic apoptosis.
analysis indicates PSF (show IL-3 Antibodies) within the PER complex recruits SIN3A (show SIN3A Antibodies), a scaffold for assembly of transcriptional inhibitory complexes, and the PER complex thereby rhythmically delivers histone deacetylases to the Per1 (show PER1 Antibodies) promoter, which repress Per1 (show PER1 Antibodies) transcription
Basal and cyclic AMP (show TMPRSS5 Antibodies)-induced Rbp4 (show RBP4 Antibodies) transcription is regulated by a multiprotein complex that is similar to ones that modulate expression of genes of steroid hormone biosynthesis.
identified as a protein kinase (show CDK7 Antibodies) Calpha (show PRKACA Antibodies)-binding protein in the cell nucleus
This gene encodes component A of the RAB geranylgeranyl transferase holoenzyme. In the dimeric holoenzyme, this subunit binds unprenylated Rab GTPases and then presents them to the catalytic Rab GGTase subunit for the geranylgeranyl transfer reaction. Rab GTPases need to be geranylgeranyled on either one or two cysteine residues in their C-terminus to localize to the correct intracellular membrane. Mutations in this gene are a cause of choroideremia\; also known as tapetochoroidal dystrophy (TCD). This X-linked disease is characterized by progressive dystrophy of the choroid, retinal pigment epithelium and retina. Alternative splicing results in multiple transcript variants encoding different isoforms.
Rab escort protein 1
, rab proteins geranylgeranyltransferase component A 2
, choroideremia (Rab escort protein 1)
, choroideremia protein
, rab proteins geranylgeranyltransferase component A 1
, choroideraemia protein homolog
, choroideremia protein homolog
, rab escort protein 1
, DNA-binding p52/p100 complex, 100 kDa subunit
, PTB-associated splicing factor
, PTB-associated-splicing factor
, polypyrimidine tract-binding protein-associated-splicing factor
, splicing factor, proline- and glutamine-rich