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Human GDNF Protein expressed in Escherichia coli (E. coli) - ABIN1686334
Pelletier, Lagacé, St-Amour, Arsenault, Cisbani, Chabrat, Fecteau, Lévesque, Cicchetti: The morphological and molecular changes of brain cells exposed to direct current electric field stimulation. in The international journal of neuropsychopharmacology / official scientific journal of the Collegium Internationale Neuropsychopharmacologicum (CINP) 2015
Results provide evidence that uPA (show PRAP1 Proteins) and IGF1R (show IGF1R Proteins) directly interact with uPAR (show PLAUR Proteins) enhancing malignant potential of triple-negative breast cancer.
suggest that the low endogenous levels of uPA (show PRAP1 Proteins) in blood are actively regulated, and that the regulatory mechanisms are disrupted in QPD in a megakaryocyte-specific manner
an intricate link between caveolin-1 (show CAV1 Proteins) and Src kinase (show CSK Proteins)-mediated cell signaling and alveolar epithelial cell apoptosis due to loss of SP-C (show SFTPC Proteins) expression through p53 (show TP53 Proteins) and uPA (show PRAP1 Proteins) system-mediated cross-talk, is reported.
there is a decrease in epidermal GDNF and GFRalpha-1 protein expression in normal human skin with ageing
In SOD1(G93A) spinal cords, we verified a strict correlation in the expression of the TNFalpha, TNFR1 and GDNF triad at different stages of disease progression. Yet, ablation of TNFR1 completely abolished GDNF rises in both SOD1(G93A) astrocytes and spinal cords, a condition that accelerated motor neuron degeneration and disease progression
results show that the uPA (show PRAP1 Proteins)/uPAR (show PLAUR Proteins)/LRP1 (show LRP1 Proteins) system is a potential target for the development of therapeutic strategies to promote axonal recovery following a CNS injury
In functional dyspepsia patients, duodenal expression of GDNF protein was significantly increased compared with controls. GDNF was localized in enteric glial cells, eosinophils, and epithelial cells.
The present research concluded that aspirin suppressed prostate cancer cell invasion by reducing MMP-9 (show MMP9 Proteins) activity and uPA (show PRAP1 Proteins) expression through decreasing of IKK-beta (show IKBKB Proteins)-mediated NF-kappaB (show NFKB1 Proteins) activation, indicating that the ability of aspirin to inhibit cell invasion might be useful in the chemoprevention of metastatic prostate cancer.
Suppression of miR-383 may increase the therapeutic potential of human bone-marrow-derived MSCs in treating spinal cord injury via augmentation of GDNF protein levels.
These studies identify uPA (show PRAP1 Proteins)-dependent de-repression of vegfr1 (show FLT1 Proteins) and vegfr2 (show KDR Proteins) gene transcription through binding to HHEX/PRH (show HHEX Proteins) as a novel mechanism by which uPA (show PRAP1 Proteins) mediates the pro-angiogenic effects of VEGF (show VEGFA Proteins) and identifies a potential new target for control of pathologic angiogenesis.
results contradict previous studies suggesting that mammalian GFRalpha1 (show GFRA1 Proteins) and GDNF cannot bind and activate non-mammalian RET (show RET Proteins) and vice versa
the dynamics of glial cell line-derived neurotrophic factor (gdnf) and nitric oxide synthases (nos) mRNA expression in various regions of zebrafish brain
GDNF family ligands including tyrosine kinase receptor (show KDR Proteins) RET (show RET Proteins) are investigated within the adult zebrafish brain.
GDNF is a major determinant of directed neuritic growth , and GDNF acts by promoting local neurite outgrowth.
These results demonstrated the expression of the GDNF receptorial complex in adult zebrafish cerebellum and suggest an autocrine mode of action of GDNF in Purkinje cells.
These results showed that the expression of GDNF is not probably restricted during development but it might be involved in the physiology of adult zebrafish retina.
The expression of glial cell line-derived neurotrophic factor (GDNF) was not restricted to developmental periods but it seems that this factor might be involved in adult zebrafish brain physiology, as observed in mammals.
Analysis of striatal brain samples confirms increased GDNF expression in lentiviral vector-GDNF treated aged animals that correlates with functional improvements and preserved dopaminergic markers, dependent upon GDNF levels.
Ret (show RET Proteins) is essential to mediate GDNF's neuroprotective and neuroregenerative effect in a Parkinson disease mouse model.
identified IFNg (show IFNG Proteins), Neurturin (Nrtn (show NRTN Proteins)), and glial-derived neurotrophic factor (GDNF) as ligands with unexpected roles in promoting neurogenic differentiation (show NEUROD1 Proteins) of Neural Precursor Cells in vivo.
Using an organ culture system for prostate development and Ret mutant mice, we demonstrate that RET-mediated GDNF signaling in UGS increases proliferation of mesenchyme cells and suppresses androgen-induced proliferation and differentiation of prostate epithelial cells, inhibiting prostate development.
The GDNF-GFRalpha1 (show GFRA1 Proteins) complex is essential for proper hippocampal circuit development.
GDNF signals were able to induce the stratified aggregate formation of GFRalpha1 (show GFRA1 Proteins)-positive undifferentiated spermatogonia
Our results show the existence of two subpopulations of peptidergic nociceptors characterized by the presence of CGRP (show CALCA Proteins), one expressing BDNF (show BDNF Proteins) (plus SP), the other expressing GDNF (plus SST (show SST Proteins)), suggesting a different role for these two neurotrophic factors in the discrimination of specific painful stimuli modalities.
The data of this study suggested that short-term exposure to hyperoxic conditions can affect the regulation and expression of BDNF (show BDNF Proteins) potentially leading to alterations in neural development.
The Gdnf cKO males sired up to two litters but became infertile due to collapse of spermatogenesis and loss of undifferentiated spermatogonia
Our results reveal the role of GDNF in nigrostriatal dopamine system postnatal development and adult function, and highlight the importance of correct spatial expression of GDNF
Spatial expression analysis by whole-mount in situ hybridization showed that the GDNF mRNA was predominantly detected in somites, pronephros, pharyngeal arches, epibranchial placodes, digestive tract and some of the lateral line structure.
This gene encodes a highly conserved neurotrophic factor. The recombinant form of this protein was shown to promote the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. Multiple transcript variants encoding different isoforms have been found for this gene. Mutations in this gene may be associated with Hirschsprung disease.
, plasminogen activator, urinary
, urokinase-type plasminogen activator
, Glial cell line derived neutrophic factor
, astrocyte-derived trophic factor
, glial cell line derived neurotrophic factor
, glial cell line-derived neurotrophic factor
, glial cell line-derived neurotrophic factor long form
, glial cell derived neurotrophic factor
, glial cell-line derived neurotrophic factor
, neurotrophic factor
, glial cell line-derived neurotrophic factor a
, glia-derived neurotrophic growth factor